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	<title><![CDATA[BOL: Related items]]></title>
	<link>https://bioinformaticsonline.com/related/45349?offset=1580</link>
	<atom:link href="https://bioinformaticsonline.com/related/45349?offset=1580" rel="self" type="application/rss+xml" />
	<description><![CDATA[]]></description>
	
	
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  <guid isPermaLink='true'>https://bioinformaticsonline.com/opportunity/view/22431/genomic-scientist-at-udsc</guid>
  <pubDate>Thu, 28 May 2015 19:14:23 -0500</pubDate>
  <link></link>
  <title><![CDATA[Genomic Scientist at UDSC]]></title>
  <description><![CDATA[
<p>Centre for Genetic Manipulation of Crop Plants</p>

<p>Department of Genetics</p>

<p>University of Delhi South Campus</p>

<p>NEW DELHI – 110 021</p>

<p>WALK-IN-INTERVIEW FOR THE TEMPORARY POSITIONS OF RESEACH SCIENTIT &amp; LAB / FIELD ATTENDANT</p>

<p>1 Research Scientist (RS) – 3</p>

<p>    DBT, Ph. D.</p>

<p>    Experience on DNA Markers, plant genome mapping and bioinformatics</p>

<p>    Salary: 60,000 (Consolidated) + 5% annual increment</p>

<p>    Date and time: 25.06.2015 at 10:30 AM</p>

<p>These temporary positions have been sanctioned in a DBT funded project for the Phase II on ‘Centre of Excellence on genome mapping and molecular breeding of Brassicas.’</p>

<p>The applicants are requested to register their names on the day of interview in the First Floor, Biotech Centre, Centre for Genetic Manipulation of Crop Plants, Department of Genetics before the stipulated time for the interview. Only the registered eligible candidates will be interviewed on the day in the Committee Room.</p>

<p>Applicants are requested to bring all related documents, in original and a set of photocopy, for verification.</p>

<p>No TA/DA will be paid for attending the interview.</p>

<p>Advertisement:</p>

<p>www.du.ac.in/du/index.php?mact=News,cntnt01,detail,0&amp;cntnt01articleid=5492&amp;cntnt01returnid=83</p>
]]></description>
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	<guid isPermaLink="true">https://bioinformaticsonline.com/blog/view/45306/the-genes-that-travel-together-a-genomic-detective-story</guid>
	<pubDate>Fri, 11 Sep 2026 13:00:36 -0500</pubDate>
	<link>https://bioinformaticsonline.com/blog/view/45306/the-genes-that-travel-together-a-genomic-detective-story</link>
	<title><![CDATA[The Genes That Travel Together: A Genomic Detective Story]]></title>
	<description><![CDATA[<p>Imagine looking through thousands of microbial genomes and discovering two genes that repeatedly appear together. The obvious conclusion is that they must somehow be connected&mdash;that perhaps they work together, participate in the same pathway, or depend on each other. But evolution has a way of leaving misleading clues. What if these two genes are found together simply because they were inherited from the same ancient ancestor? In that case, their apparent association may have little to do with their biological function; it may simply be a reflection of shared evolutionary history. This is the intriguing problem addressed by CORGIAS (https://github.com/ynishimuraLv/corgias), a computational framework developed to distinguish genuine gene associations from correlations created by common ancestry.</p><p>Instead of asking only whether two genes occur together across genomes, CORGIAS asks a deeper question: did these genes actually evolve together, repeatedly gaining or losing their presence in concert, or are they merely travelling together because of their inherited history? The framework introduces two complementary approaches, Ancestral State Adjustment (ASA) and the Simultaneous EVolution test (SEV), which incorporate evolutionary information into the search for gene associations. This distinction becomes increasingly important as genome sequencing continues to uncover enormous numbers of microbial genomes, many from organisms that have never been cultured and whose genes remain functionally mysterious. In this growing genomic landscape, simply finding a gene is no longer enough&mdash;we need clues about what that gene might be doing. CORGIAS approaches this problem almost like a genomic detective: rather than treating every association as evidence, it reconstructs the evolutionary story behind the association and asks whether the evidence survives that history. By doing so, it offers a way to separate coincidence from biological connection and potentially uncover functional relationships hidden within the vast microbial genomic landscape. The broader message is beautifully simple: genes do not evolve in isolation, and understanding what they do may require us to look beyond where they are today and reconstruct how they arrived there. Sometimes, the most important clue in a genome is not the gene itself, but the evolutionary journey it has taken.</p><p>More at&nbsp;https://academic.oup.com/nargab/article/7/4/lqaf182/8377910?</p>]]></description>
	<dc:creator>BioStar</dc:creator>
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  <guid isPermaLink='true'>https://bioinformaticsonline.com/opportunity/view/22432/walk-ins-for-jrf-ans-srf-post-in-assam-agricultural-university</guid>
  <pubDate>Thu, 28 May 2015 19:16:47 -0500</pubDate>
  <link></link>
  <title><![CDATA[Walk-ins for JRF ans SRF post in Assam Agricultural University]]></title>
  <description><![CDATA[
<p>Distributed Information Centre<br />Department of Agricultural Biotechnology<br />Assam Agricultural University<br />Jorhat – 785 013<br />Walk-in interview</p>

<p>(ABT/DIC/01/2014 (No. AAU/ABT/DIT/Advt. 01/2015/111 Dtd. 19-05-2015)</p>

<p>Walk in interview for the following position will be held on 6th June, 2015 at 10.00AM in the Office Chamber of the undersigned. Candidates may appear for the interview with bio-data, reprints / publication / thesis etc and passport size photographs, original and attested copies of all testimonials etc, which must be presented at the time of interview. The applicants may submit their resume in advance tomkmodi@aau.ac.in.</p>

<p>Research Associate</p>

<p>    Ph.D. in Biotechnology/ Bioinformatics. Or</p>

<p>    Masters degree in Biotechnology/Bioinformatics with minimum 3(three) years research experience</p>

<p>    Desirable : Experience in Bioinformatics as evidenced from published research</p>

<p>    Rs 36,000+HRA for the 1st two years and 38,000+HRA for the 3rd year.</p>

<p>Senior Research Fellow</p>

<p>    Master Degree in Biotechnology/ Bioinformatics. With 2 (two) years  Experience in Bioinformatics as evidenced from Course work/ Diploma/Published research</p>

<p>    Rs 28,000+HRA for NET qualified candidate/Professional degree holder</p>

<p>    Rs 18,000+HRA for non-NET qualified general degree holder</p>

<p>Junior Research Fellow</p>

<p>    Master Degree in Biotechnology/ Bioinformatics/Computer Science/Computer Application</p>

<p>    Desirable: Experience in Bioinformatics as evident from Course work/ Diploma/Published research</p>

<p>    Rs 25,000+HRA for NET qualified candidate/Professional degree holder</p>

<p>    Rs 16,000+HRA for non-NET qualified general degree holder</p>

<p>Note: Term and conditions will be as per the DBT, Govt of India guidelines.</p>

<p>Advertisement: http://14.139.222.145/classified/biotech46.html</p>
]]></description>
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  <guid isPermaLink='true'>https://bioinformaticsonline.com/opportunity/view/11798/phd-scholarship-denmark</guid>
  <pubDate>Fri, 13 Jun 2014 13:44:07 -0500</pubDate>
  <link></link>
  <title><![CDATA[PHD SCHOLARSHIP DENMARK]]></title>
  <description><![CDATA[
<p>ne PhD position is available at the Bioinformatics Center, Department of Biology, University of Copenhagen, Denmark. The PhD position concerns protein structure prediction, and will be in the Structural Bioinformatics group of Associate professor Thomas Hamelryck. The group is an integrated part of the Bioinformatics Center, which is headed by Professor Anders Krogh, employs around sixty scientists (including PhD students) and focuses on non-coding RNA, eukaryotic gene regulation and protein structure prediction. The center provides a modern, pleasant, international working environment with excellent modern facilities, in the heart of Copenhagen.<br />The project will be supervised by Associate Professor Thomas Hamelryck.</p>

<p>The protein folding problem is of enormous practical, theoretical and medical importance - and in addition forms a fascinating intellectual challenge. The aim of this project is to develop and implement a probabilistic method to infer the structure of proteins, building on various probabilistic models of protein structure developed by the Hamelryck group. The method will also take the dynamic nature of proteins into account, and involves a close collaboration with the statistics department at the university within the interdisciplinary project "Dynamical Systems: Mathematical Modeling and Statistical Methods for the Social, Health, and Natural Sciences" (http://dsin.ku.dk/).</p>

<p>Qualifications<br />Knowledge of programming (C++) and statistics or machine learning. Knowledge of biology, physics or biophysics is a plus, but not a requirement.</p>

<p>The deadline for applications is June 15, 2014</p>

<p>More at : https://job.jobnet.dk/CV/FindJob/details.aspx/3695051%20</p>
]]></description>
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  <guid isPermaLink='true'>https://bioinformaticsonline.com/opportunity/view/22512/srf-post-in-nehu-shillong</guid>
  <pubDate>Wed, 03 Jun 2015 13:15:38 -0500</pubDate>
  <link></link>
  <title><![CDATA[SRF post in NEHU, Shillong]]></title>
  <description><![CDATA[
<p>Dept of Biochemistry <br />North-Eastern Hill University<br />(A University with Potential for Excellence) <br />Umshing, Shillong- 793 022</p>

<p>Applications are invited for the post of Senior Research Fellow- SRF (1) and Junior Research Fellow- JRF (1) to be appointed in a SERB-funded major research project entitled “Biochemical and functional properties of Synechocystis Glutathione S-transferase(s)” sanctioned to Dr. Timir Tripathi, Molecular and Structural Biophysics Laboratory, Department of Biochemistry, NEHU, Shillong. </p>

<p>Essential Qualifications: For both positions M.Sc. or equivalent with a good academic record is a prerequisite. </p>

<p>For Project-SRF, experience in bioinformatics/computational biology is required, which should be evident by atleast one good publication. </p>

<p>For JRF position, freshers can also apply. </p>

<p>Stipend: As per SERB norms. </p>

<p>Interested students can email their detailed bio-data including mobile number and recent photograph to msb.biochem@gmail.com, latest by 20.06.15. The hard copy is not required. The date of interview will be informed after primary scrutiny of the applications. No TA/DA will be paid if called for interview. For details of the research work of the PI’s group kindly visit www.ttripathi.webs.com</p>

<p>Advertisement: http://www.nehu.ac.in/Advertisements/BiochemSERB_Advt_020615.pdf</p>
]]></description>
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	<guid isPermaLink="true">https://bioinformaticsonline.com/bookmarks/view/36846/gblocks-eliminates-poorly-aligned-positions-and-divergent-regions-of-a-dna-or-protein-alignment</guid>
	<pubDate>Sat, 02 Jun 2018 07:36:05 -0500</pubDate>
	<link>https://bioinformaticsonline.com/bookmarks/view/36846/gblocks-eliminates-poorly-aligned-positions-and-divergent-regions-of-a-dna-or-protein-alignment</link>
	<title><![CDATA[Gblocks: eliminates poorly aligned positions and divergent regions of a DNA or protein alignment]]></title>
	<description><![CDATA[<p><a href="http://molevol.cmima.csic.es/castresana/Gblocks.html">Gblocks</a><span>&nbsp;eliminates poorly aligned positions and divergent regions of a DNA or protein alignment so that it becomes more suitable for phylogenetic analysis. This server implements the most important features of the Gblocks program to make its use as simple as possible without loosing the functionality that it is necessary in most of the cases. Other options can be changed in the stand-alone program. You can see here an&nbsp;</span><a href="http://molevol.cmima.csic.es/castresana/Gblocks_server/nad3.pir-gb.htm">example output file</a><span>&nbsp;showing the blocks selected from a protein alignment. Further information can be found in the&nbsp;</span><a href="http://molevol.cmima.csic.es/castresana/Gblocks/Gblocks_documentation.html">online documentation</a><span>.&nbsp;</span></p><p>Address of the bookmark: <a href="http://molevol.cmima.csic.es/castresana/Gblocks_server.html" rel="nofollow">http://molevol.cmima.csic.es/castresana/Gblocks_server.html</a></p>]]></description>
	<dc:creator>Poonam Mahapatra</dc:creator>
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	<guid isPermaLink="true">https://bioinformaticsonline.com/pages/view/22569/reverse-complement-problem-solved-with-perl</guid>
	<pubDate>Tue, 09 Jun 2015 23:37:23 -0500</pubDate>
	<link>https://bioinformaticsonline.com/pages/view/22569/reverse-complement-problem-solved-with-perl</link>
	<title><![CDATA[Reverse Complement Problem Solved with Perl]]></title>
	<description><![CDATA[<p>Question at http://rosalind.info/problems/1b/</p><p>#Find the reverse complement of a DNA string.<br />#Given: A DNA string Pattern.<br />#Return: Pattern, the reverse complement of Pattern.<br /><br />use strict;<br />use warnings;<br /><br />my $string="AAAACCCGGT";<br />my $finalString="";<br />my %hash = (<br />&nbsp;&nbsp; &nbsp;"C" =&gt; "G", <br />&nbsp;&nbsp; &nbsp;"A" =&gt; "T", <br />&nbsp;&nbsp; &nbsp;"T" =&gt; "A", <br />&nbsp;&nbsp; &nbsp;"G" =&gt; "C",<br />);<br /><br />for (my $aa=0; $aa&lt;=(length($string)-1); $aa++) {<br />&nbsp;&nbsp; &nbsp;my $char=substr $string, $aa, 1;<br />&nbsp;&nbsp; &nbsp;#print $hash{$char};<br />&nbsp;&nbsp; &nbsp;$finalString="$hash{$char}"."$finalString";<br />}<br /><br />print $finalString;<br />print "\n";</p>]]></description>
	<dc:creator>Jit</dc:creator>
</item>
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	<guid isPermaLink="true">https://bioinformaticsonline.com/blog/view/38238/list-of-motif-discovery-tools</guid>
	<pubDate>Tue, 20 Nov 2018 03:54:26 -0600</pubDate>
	<link>https://bioinformaticsonline.com/blog/view/38238/list-of-motif-discovery-tools</link>
	<title><![CDATA[List of motif discovery tools !]]></title>
	<description><![CDATA[<div><div>In genetics, a sequence motif is a nucleotide or amino-acid sequence pattern that is widespread and has, or is conjectured to have, a biological significance. For proteins, a sequence motif is distinguished from a structural motif, a motif formed by the three-dimensional arrangement of amino acids which may not be adjacent.</div><div>&nbsp;</div><div>Following are the list of tools for motif discovery:</div><div>&nbsp;</div><div><a href="http://genius.embnet.dkfz-heidelberg.de/menu/biounit/open-husar/">2Dsweep -- protein annotation by secondary structure elements</a></div><p>Perform secondary structure predictions on protein sequences.</p></div><div><div><a href="http://floresta.eead.csic.es/3dfootprint/">3D-footprint -- database of DNA-binding protein structures</a></div><p>Find binding specificity information about DNA-protein complexes.</p></div><div><div><a href="http://floresta.eead.csic.es/3dfootprint/">3D-footprint: DNA-binding protein database</a></div><p>Find information about the binding specificity of DNA-binding proteins.</p></div><div><div><a href="http://3d-partner.life.nctu.edu.tw/">3D-partner -- a web server to infer interacting partners and binding models</a></div><p>Predict interacting partners and binding models.</p></div><div><div><a href="http://motif.stanford.edu/distributions/3motif/">3MOTIF -- a protein structure visualization system for conserved sequence motifs</a></div><p>Use this web-based sequence motif visualization system to display sequence motif information in its appropriate three-dimensional (3D) context.</p></div><div><div><a href="http://bioinfo.mpiz-koeln.mpg.de/afawe/">AFAWE -- Automatic functional annotation in a distributed Web Services Environment</a></div><p>Protein function prediction and annotation in an integrated environment powered by web service.</p></div><div><div><a href="http://anchor.enzim.hu/">ANCHOR -- Prediction of Protein Binding Regions in Disordered Proteins</a></div><p>Find information about protein binding.</p></div><div><div><a href="http://annie.bii.a-star.edu.sg/annie/home.do">ANNIE -- ANNotation and Interpretation Environment for Protein Sequences</a></div><p>Use to predict function from de novo protein sequences.</p></div><div><div><a href="http://bioinformatica.isa.cnr.it/ASC/">Active Sequences Collection (ASC) database -- A new tool to assign functions to protein sequences</a></div><p>Search for short active protein sequences with demonstrated biological activities.</p></div><div><div><a href="http://blocks.fhcrc.org/">Blocks -- Ungapped segments in conserved protein sequences</a></div><p>Search for ungapped segments corresponding to the most highly conserved regions of proteins.</p></div><div><div><a href="http://cast.engr.uic.edu/">CASTp -- computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues</a></div><p>Identify and measure surface accessible pockets as well as interior inaccessible cavities, for proteins and other molecules.</p></div><div><div><a href="http://www.ebi.ac.uk/thornton-srv/databases/CSA">CSA -- The Catalytic Site Atlas</a></div><p>To search for catalytic residue annotation for enzymes in the Protein Data Bank.</p></div><div><div><a href="http://www.sbg.bio.ic.ac.uk/~confunc/">ConFunc -- Conserved residue Protein Function Prediction Server</a></div><p>Predict protein function using Gene Ontology.</p></div><div><div><a href="http://consurf.tau.ac.il/">ConSurf-DB -- evolutionary conservation profiles of protein structures database</a></div><p>Automatically calculate evolutionary conservation scores of key amino acid residues and map them on protein structures.</p></div><div><div><a href="http://salilab.org/DBAli/">DBAli -- A Database of Structure Alignments</a></div><p>Mine the protein structure space.</p></div><div><div><a href="http://dilimot.embl.de/">DILIMOT -- discovery of linear motifs in proteins</a></div><p>Predict short linear motifs (3-8 residues) in a set of protein sequences.</p></div><div><div><a href="http://www.ebi.ac.uk/dasty/">Dasty2 -- an Ajax protein DAS client</a></div><p>A web client for visualizing protein sequence feature information using DAS.</p></div><div><div><a href="http://genius.embnet.dkfz-heidelberg.de/menu/biounit/open-husar/">DomainSweep -- protein annotation by domain analysis</a></div><p>Identify the domain architecture within a protein sequence.</p></div><div><div><a href="http://e1ds.csbb.ntu.edu.tw/">E1DS -- catalytic site prediction based on 1D signatures of concurrent conservation</a></div><p>Predict enzyme catalytic site.</p></div><div><div><a href="http://elm.eu.org/">ELM -- Eukarotic Linear Motif Resource</a></div><p>Predict functional sites in eukaryotic proteins.</p></div><div><div><a href="http://us.expasy.org/tools/#proteome">EXPASY Proteome Tools Collection</a></div><p>Use a collection of tools for protein analyses.</p></div><div><div><a href="http://us.expasy.org/tools/findmod/">EXPASY-Findmod</a></div><p>Predict potential protein post-translational modifications and find potential single amino acid substitutions in peptides.</p></div><div><div><a href="http://mbs.cbrc.jp/EzCatDB/">EzCatDB -- the Enzyme Catalytic-mechanism Database</a></div><p>Search for information related to the catalytic mechanisms of enzymes.</p></div><div><div><a href="http://bioinf.cs.ucl.ac.uk/ffpred/">FFPred -- feature-based function prediction</a></div><p>An integrated feature-based function prediction server for vertebrate proteomes.</p></div><div><div><a href="http://www.ebi.ac.uk/printsscan/">FingerPRINT Scan</a></div><p>Identify the closest matching PRINTS sequence motif fingerprints in a protein sequence.</p></div><div><div><a href="http://firedb.bioinfo.cnio.es/">FireDB -- a database of functionally important residues from proteins of known structure</a></div><p>Search for functional annotation of important sites in proteins with known structures.</p></div><div><div><a href="http://bioserv.rpbs.univ-paris-diderot.fr/cgi-bin/Frog2">Frog2 -- a FRee Online druG 3D conformation generator</a></div><p>Produce 3D conformations of small drug compounds.</p></div><div><div><a href="http://www.hgpd.jp/">HGPD -- Human Gene and Protein Database</a></div><p>A database presenting experiment-based results in human proteomics.</p></div><div><div><a href="http://hhsenser.tuebingen.mpg.de/">HHsenser -- exhaustive transitive profile search using HMMx96HMM comparison</a></div><p>Conduct exhaustive intermediate profile searches of a set of homologous protein sequences.</p></div><div><div><a href="http://loschmidt.chemi.muni.cz/hotspotwizard/">HotSpot Wizard -- Substrate Specificity Hot Spot Identification web server</a></div><p>Design protein mutations in site-directed mutagenesis.</p></div><div><div><a href="http://phylogenomics.berkeley.edu/intrepid/">INTREPID -- INformation-theoretic TREe traversal for Protein functional site IDentification</a></div><p>Use for protein functional site identification.</p></div><div><div><a href="http://www.cbs.dtu.dk/">Integrating protein annotation resources through the Distributed Annotation System</a></div><p>Annotate protein using this integrated annotation resource.</p></div><div><div><a href="http://www.ebi.ac.uk/InterProScan/">InterProScan -- protein domains identifier</a></div><p>Identify protein family (and DNA) domains, patterns, motifs, protein families, and functional sites.</p></div><div><div><a href="http://kfc.mitchell-lab.org/">KFC -- Knowledge-based FADE and Contacts</a></div><p>Interactive forecasting of protein interaction hot spots.</p></div><div><div><a href="http://biominer.bime.ntu.edu.tw/magiicpro/">MAGIIC-PRO -- detecting functional signatures by efficient discovery of long patterns in protein sequences</a></div><p>Discover long patterns in protein sequences.</p></div><div><div><a href="http://prodata.swmed.edu/malisam">MALISAM -- Manual ALIgnments for Structurally Analogous Motifs</a></div><p>Database containing pairs of structural analogs and their alignments.</p></div><div><div><a href="http://meme.nbcr.net/">MEME -- discovering and analyzing DNA and protein sequence motifs</a></div><p>Find sequence patterns in DNA and protein sequences.</p></div><div><div><a href="http://www.nii.res.in/modpropep.html">MODPROPEP -- a program for knowledge-based modeling of protein-peptide complexes</a></div><p>A web server for knowledge-based modeling of protein-peptide complexes, specifically peptides in complex with major histocompatibility complex (MHC) proteins and kinases.</p></div><div><div><a href="http://www.bioinfo.tsinghua.edu.cn/~tigerchen/memo.html">MeMo -- a web tool for prediction of protein methylation modifications</a></div><p>Predict protein methylation sites.</p></div><div><div><a href="http://caps.ncbs.res.in/MegaMotifbase/index.html">MegaMotifBase -- a database of structural motifs in protein families and superfamilies</a></div><p>Find structural segments or motifs for protein structures.</p></div><div><div><a href="http://mnm.engr.uconn.edu/MNM/SMSSearchServlet">Minimotif Miner -- a tool for investigating protein function</a></div><p>Find motifs in a protein sequence.</p></div><div><div><a href="http://umber.sbs.man.ac.uk/dbbrowser/motif3d/motif3d.html">Motif3D -- Relating protein sequence motifs to 3D structure</a></div><p>Visualize protein sequence motifs on the 3D protein structures.</p></div><div><div><a href="http://myhits.isb-sib.ch/cgi-bin/motif_scan">MotifScan</a></div><p>Find presence of any known protein motif (Prosite and Pfam) in a protein sequence.</p></div><div><div><a href="http://bioinfo3d.cs.tau.ac.il/MultiBind">MultiBind -- Multiple Alignment of Protein Binding Sites</a></div><p>Recognize spatial chemical binding patterns common to a set of protein structures.</p></div><div><div><a href="http://mendel.imp.univie.ac.at/myristate/SUPLpredictor.htm">NMT -- The MYR Predictor</a></div><p>Analyze proteins for the presence of N-terminal N-myristoylation site.</p></div><div><div><a href="http://www.cbs.dtu.dk/services/NetNGlyc/">NetNGlyc -- N-Glycosylation sites prediction tool</a></div><p>Find the presence of N-Glycosylation sites in human proteins.</p></div><div><div><a href="http://www.cbs.dtu.dk/services/NetOGlyc/">NetOGly 3.1 -- O-glycosylation sites prediction tool</a></div><p>Find the presence of O-GalNAc (mucin type) glycosylation sites in mammalian proteins.</p></div><div><div><a href="http://www.cbs.dtu.dk/services/NetPhos/">NetPhos 2.0 -- Phosphorylation sites predictions</a></div><p>Analyze eukaryotic proteins for the presence of serine, threonine and tyrosine phosphorylation sites.</p></div><div><div><a href="http://www.cbs.dtu.dk/services/NetPhosK/">NetPhosK 1.0 Server -- kinase specific eukaryotic protein phosphorylation sites prediction tool</a></div><p>Find possible kinase specific phosphorylation sites in eukaryotic proteins.</p></div><div><div><a href="http://networkin.info/search.php">NetworKIN -- a resource for exploring cellular phosphorylation networks</a></div><div>&nbsp;</div></div><div><div><a href="http://neuroproteomics.scs.uiuc.edu/neuropred.html">NeuroPred -- a tool to predict cleavage sites in neuropeptide precursors and provide the masses of the resulting peptides</a></div><p>Predict cleavage sites at basic amino acid locations in neuropeptide precursor sequences.</p></div><div><div><a href="http://www.ebi.ac.uk/patentdata/nr/">Non-Redundant Patent Sequences - Patented Sequence Database</a></div><p>Find information about patented nucleotide and protein sequences.</p></div><div><div><a href="http://www.cbs.dtu.dk/databases/OGLYCBASE/">O-GLYCBASE</a></div><p>Search for information about glycoproteins with O-linked and C-linked glycosylation sites.</p></div><div><div><a href="http://www.pandora.cs.huji.ac.il/">PANDORA -- Protein ANnotation Diagram ORiented Analysis</a></div><p>Find information about protein sequence annotations.</p></div><div><div><a href="http://sunserver.cdfd.org.in:8080/protease/PAR_3D/index.html">PAR-3D -- Protein Active site Residue - 3D structural motif</a></div><p>A server to predict protein active site residues.</p></div><div><div><a href="http://wwwmgs.bionet.nsc.ru/mgs/gnw/pdbsite/">PDBSite -- a database of the 3D structure of protein functional sites</a></div><p>Search for structural and functional information on the protein functional sites.</p></div><div><div><a href="http://wwwmgs.bionet.nsc.ru/mgs/systems/fastprot/pdbsitescan.html">PDBSiteScan -- A program for searching for active, binding and posttranslational modification sites in the 3D structures of proteins</a></div><p>Search 3D protein fragments similar in structure to known active, binding and posttranslational modification sites.</p></div><div><div><a href="http://pedant.gsf.de/">PEDANT -- Protein Extraction, Description and ANalysis Tool</a></div><p>Conduct genome wide functional and structural analysis.</p></div><div><div><a href="http://phosida.org/">PHOSIDA -- Phosphorylation site database</a></div><p>Search for phosphorylation data of any protein of interest.</p></div><div><div><a href="http://www.phosphorylation.biochem.vt.edu/">PHOSPHORYLATION SITE DATABASE</a></div><p>Search for information on prokaryotic proteins that undergo serine, threonine, or tyrosine phosphorylation.</p></div><div><div><a href="http://www.jcvi.org/pn-utility/web/smarty_wrapper/about.php">PNU -- Protein Naming Utility</a></div><p>Determine correct names for proteins.</p></div><div><div><a href="http://mbs.cbrc.jp/poodle/poodle-s.html">POODLE-S -- Predicition Of Order and Disorder by machine LEarning</a></div><p>Web application for predicting protein disorder by using physicochemical features and reduced amino acid set of a position-specific scoring matrix.</p></div><div><div><a href="http://gemdock.life.nctu.edu.tw/ppisearch/">PPISearch -- Protein-Protein Interaction Search</a></div><p>Find homologous protein-protein interactions across multiple species.</p></div><div><div><a href="http://www.ebi.ac.uk/ppsearch/">PPSearch</a></div><p>Search your query sequence against PROSITE pattern database for protein motifs.</p></div><div><div><a href="http://pridb.gdcb.iastate.edu/">PRIDB -- Protein-RNA Interface DataBase</a></div><p>Find information about protein-RNA complexes from the Protein Data Bank (PDB).</p></div><div><div><a href="http://umber.sbs.man.ac.uk/dbbrowser/PRINTS/">PRINTS and its automatic supplement, prePRINTS -- A compendium of protein fingerprints</a></div><p>Search for protein fingerprints.</p></div><div><div><a href="http://www.expasy.org/prosite/">PROSITE</a></div><p>Identify protein families and domains for a given protein sequence.</p></div><div><div><a href="http://www.imtech.res.in/raghava/prrdb/">PRRDB -- Pattern Recognition Receptor Database</a></div><p>A comprehensive database of pattern-recognition receptors and their ligands.</p></div><div><div><a href="http://www.arabidopsis.org/cgi-bin/patmatch/nph-patmatch.pl">PatMatch -- a program for finding patterns in peptide and nucleotide sequences</a></div><p>Search for short nucleotide or peptide sequences such as cis-elements in nucleotide sequences or small domains and motifs in protein sequences.</p></div><div><div><a href="http://pepcyber.umn.edu/PPEP/">PepCyber:P~PEP -- a database of human protein protein interactions mediated by phosphoprotein-binding domains</a></div><p>Database specialized in documenting human PPBD-containing proteins and PPBD-mediated interactions.</p></div><div><div><a href="http://us.expasy.org/tools/peptidecutter/">PeptideCutter -- protein cleavage sites prediction tool</a></div><p>Predicts potential protease cleavage sites and sites cleaved by chemicals in a given protein sequence.</p></div><div><div><a href="http://phobius.binf.ku.dk/">Phobius -- A combined transmembrane topology and signal peptide predictor</a></div><p>Predict combined transmembrane topology and signal peptides.</p></div><div><div><a href="http://phospho.elm.eu.org/">Phospho.ELM -- a database of phosphorylation sites</a></div><p>Search for eukaryotic phosphorylation sites.</p></div><div><div><a href="http://www.phospho3d.org/">Phospho3D -- a database of three-dimensional structures of protein phosphorylation sites</a></div><p>Search for 3D structure and functional annotation of phosphorylation sites in proteins.</p></div><div><div><a href="http://www.phosphosite.org/">PhosphoSite -- A bioinformatics resource dedicated to physiological protein phosphorylation.</a></div><p>Search the database of in vivo phosphorylation sites of human and mouse proteins</p></div><div><div><a href="http://pxgrid.med.monash.edu.au/polyq/">PolyQ -- Polyglutamine Database</a></div><p>Find information about polyglutamine (polyQ) repeats.</p></div><div><div><a href="http://www.ebi.ac.uk/pratt/">Pratt Protein motif and pattern discovery</a></div><p>Find the presence of protein motifs and patterns in an amino acid sequence.</p></div><div><div><a href="http://www.predisi.de/">PrediSi -- Prediction of Signal Peptides and their Cleavage Positions</a></div><p>Predict signal peptide sequences and their cleavage positions in bacterial and eukaryotic amino acid sequences.</p></div><div><div><a href="http://www.ebi.ac.uk/thornton-srv/databases/ProFunc/">ProFunc -- a server for predicting protein function from 3D structure</a></div><p>Predict protein functions based on known structures.</p></div><div><div><a href="http://bioinfo41.weizmann.ac.il/promate/promateus.html">ProMateus--an open research approach to protein-binding sites analysis</a></div><p>Predict the location of potential protein-protein binding sites for unbound proteins.</p></div><div><div><a href="http://www.proteus.cs.huji.ac.il/">ProTeus -- identifying signatures in protein termini</a></div><p>Identify short linear signatures in protein termini.</p></div><div><div><a href="http://genius.embnet.dkfz-heidelberg.de/menu/cgi-bin/w2h-open/w2h.open/w2h.startthis?SIMGO=w2h%2ewelcome">ProtSweep -- protein annotation by homology</a></div><p>Analyze and identify newly obtained protein sequences.</p></div><div><div><a href="http://protemot.csbb.ntu.edu.tw/">Protemot -- prediction of protein binding sites with automatically extracted geometrical templates</a></div><p>Predict protein binding sites in a protein sequence based on geometrical analysis of protein tertiary substructures.</p></div><div><div><a href="http://quasimotifinder.tau.ac.il/">QuasiMotiFinder -- protein annotation by searching for evolutionarily conserved motif-like patterns</a></div><p>Search for evolutionarily conserved motif-like patterns in protein sequences.</p></div><div><div><a href="http://bindr.gdcb.iastate.edu/RNABindR">RNABindR -- software for prediction of RNA binding residues in proteins</a></div><p>Web-based server for analyzing and predicting RNA binding sites in proteins.</p></div><div><div><a href="http://caps.ncbs.res.in/scanmot/scanmot.html">SCANMOT -- searching for similar sequences using a simultaneous scan of multiple sequence motifs</a></div><p>Search for similarities between proteins by simultaneous matching of multiple motifs.</p></div><div><div><a href="http://bioinf.fbb.msu.ru/SDPpred/">SDPpred -- A Tool for Prediction of Amino Acid Residues that Determine Differences in Functional Specificity of Homologous Proteins</a></div><p>Predict residues in protein sequences that determine the proteins' functional specificity.</p></div><div><div><a href="http://tamm.mit.edu/SDR/">SDR -- Specificity Determining Residues Database</a></div><p>Predict specificity-determining residues in protein families.</p></div><div><div><a href="http://bioware.ucd.ie/~slimdisc/">SLiMDisc -- Short, Linear Motif Discovery</a></div><p>Find shared motifs in proteins with a common attribute.</p></div><div><div><a href="http://sumosp.biocuckoo.org/">SUMOsp -- a web server for sumoylation site prediction</a></div><p>Conduct in silico sumoylation sites prediction.</p></div><div><div><a href="http://oxytricha.princeton.edu/SWAKK/">SWAKK -- a web server for detecting positive selection in proteins using a sliding window substitution rate analysis</a></div><p>Detect protein sequence section under positive evolution selection.</p></div><div><div><a href="http://www.expasy.org/tools/scanprosite/">ScanProsite</a></div><p>Search for motifs and patterns within protein sequences.</p></div><div><div><a href="http://www.expasy.org/tools/scanprosite/">ScanProsite -- detection of PROSITE signature matches and ProRule-associated functional and structural residues in proteins</a></div><p>Detect patterns, profiles and motifs in a protein sequence.</p></div><div><div><a href="http://scansite.mit.edu/">ScanSite 2.0 -- Proteome-wide prediction of cell signaling interactions using short sequence motifs</a></div><p>Search for motifs within proteins that are likely to be phosphorylated by specific protein kinases or bind to domains such as SH2 domains, 14-3-3 domains or PDZ domains.</p></div><div><div><a href="http://sepresa.bio-x.cn/">SePreSA -- SErver for the PREdiction of populations susceptible to Serious Adverse drug reaction</a></div><p>Find information about populations carrying polymorphisms within protein binding pockets that make them susceptible to serious adverse drug reaction (SADR).</p></div><div><div><a href="http://motif.genome.jp/">Sequence Motif Search</a></div><p>Search the presence of a motif in either amino acid sequence or nucleotide sequence.</p></div><div><div><a href="http://www.csbio.sjtu.edu.cn/bioinf/Signal-3L/">Signal-3L -- A 3-layer approach for predicting signal peptides</a></div><p>Predict signal peptides.</p></div><div><div><a href="http://www.cbs.dtu.dk/services/SignalP/">SignalP -- Machine learning approaches to the prediction of signal peptides, their cleavage sites, and other protein sorting signals</a></div><p>Predict signal peptides and their cleavage sites.</p></div><div><div><a href="http://us.expasy.org/tools/sulfinator/">Sulfinator -- tyrosine sulfation sites prediction tool</a></div><p>Predict the presence of tyrosine sulfation sites in protein sequences</p></div><div><div><a href="http://bioinf-services.charite.de/supersite/">SuperSite -- Ligand Binding Site Database</a></div><p>Look at protein structure from a ligand and binding site perspective.</p></div><div><div><a href="http://www.ch.embnet.org/">Swiss EMBnet node web server</a></div><p>Use a collection of bioinformatics tools at this portal site.</p></div><div><div><a href="http://bioinfo.montp.cnrs.fr/?r=t-reks">T-REKS -- identification of Tandem REpeats in sequences with a K-meanS based algorithm</a></div><p>Find information about tandem repeats in proteins that carry fundamental biological functions and are related to a number of human diseases.</p></div><div><div><a href="http://tmbeta-genome.cbrc.jp/TMFunction/">TMFunction -- The Functional Database of Membrane Proteins</a></div><p>Find information about functional residues in alpha-helical and beta-barrel membrane proteins.</p></div><div><div><a href="http://topdom.enzim.hu/">TOPDOM -- Conservatively Located Domains and Motifs in Transmembrane Proteins</a></div><p>Database of domains and motifs with conservative location in transmembrane proteins.</p></div><div><div><a href="http://motif.stanford.edu/distributions/emotif/">The EMOTIF database</a></div><p>Search for highly conserved and specific protein sequence motifs.</p></div><div><div><a href="http://treedetv2.bioinfo.cnio.es/treedet/index.html">TreeDet -- Predicting Functional Residues in Protein Sequence Alignments</a></div><p>Predict functional sites in protein sequence alignments use different methodologies.</p></div><div><div><a href="http://motif.bmi.ohio-state.edu/ChIPMotifs/">W-ChIPMotifs -- ChIP-based protein Motif discovery web server</a></div><p>Find de novo protein motifs from chromatin immunoprecipitation data.</p></div><div><div><a href="http://feature.stanford.edu/webfeature/">WebFEATURE -- an interactive web tool for identifying and visualizing functional sites on macromolecular structures</a></div><p>Scan query structures for functional sites in both proteins and nucleic acids.</p></div><div><div><a href="http://wwwmgs.bionet.nsc.ru/mgs/programs/panalyst/">WebProAnalyst -- an interactive tool for analysis of quantitative structurex96activity relationships in protein families</a></div><p>Analyze quantitative structure-activity relationship of related protein families.</p></div><div><div><a href="http://motif.stanford.edu/distributions/eblocks/">eBLOCKs -- enumerating conserved protein blocks to achieve maximal sensitivity and specificity</a></div><p>Search for ungapped alignments of highly conserved regions among a protein family or superfamily.</p></div><div><div><a href="http://ef-site.hgc.jp/eF-seek/">eF-seek -- prediction of the functional sites of proteins by searching for similar electrostatic potential and molecular surface shape</a></div><p>Predict the functional sites of proteins.</p></div><div><div><a href="http://firedb.bioinfo.cnio.es/Php/FireStar.php">firestar -- prediction of functionally important residues using structural templates and alignment reliability</a></div><p>An expert system for predicting ligand-binding residues in protein structures.</p></div><div><div><a href="http://caps.ncbs.res.in/imotdb/">iMOTdb -- a comprehensive collection of spatially interacting motifs in proteins</a></div><p>Automatically identify spatially interacting motifs among distantly related proteins sharing similar folds and possessing common ancestral lineage.</p></div>]]></description>
	<dc:creator>Neel</dc:creator>
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  <guid isPermaLink='true'>https://bioinformaticsonline.com/opportunity/view/22580/appointment-of-two-traineeships-and-two-studentships-in-bioinformatics</guid>
  <pubDate>Wed, 10 Jun 2015 10:19:07 -0500</pubDate>
  <link></link>
  <title><![CDATA[Appointment of two traineeships and two studentships in Bioinformatics]]></title>
  <description><![CDATA[
<p>Jawaharlal Nehru<br />TROPICAL BOTANIC GARDEN AND RESEARCH INSTITUTE<br />An organization under the Kerala State Council for Science, Technology and Environment and<br />National Centre of Excellence, Government of India<br /> <br />Applications are invited for the appointment of two traineeships and two studentships in Bioinformatics for a period of six months sponsored by Department of Biotechnology, Government of India in the Bioinformatics Sub-DIC, Saraswathy Thangavelu Centre, JNTBGRI, Puthenthope, Thiruvananthapuram 695 586. The required qualifications and other details are given below.</p>

<p>Monthly fellowship (in rupee): 5,000/-<br />	<br />Traineeship<br />	<br />First Class M.Sc Bioinformatics/ Biotechnology/ Botany<br />	<br />Studentship: 5,000/-<br />	<br />M.Phil/M.Tech Bioinformatics/ Biotechnology/ any branch of Life Science students for doing their thesis work in the area of Bioinformatics.</p>

<p>Age limit as on 1.1.2015, 28 years. Age relaxation will be provided for SC, ST, OBC candidates as per Govt. norms.</p>

<p>Interested candidates may appear for walk-in-interview on 16th June 2015 at 10.30 am at JNTBGRI, Palode, Thiruvananthapuram. The candidate should report to the Office at Palode before 10.00 am</p>

<p>More at http://www.jntbgri.in/jntbgri/news/File0001.pdf</p>
]]></description>
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	<guid isPermaLink="true">https://bioinformaticsonline.com/bookmarks/view/44479/doubletrouble-identify-duplicated-genes-from-whole-genome-protein-sequences-and-classify</guid>
	<pubDate>Tue, 05 Mar 2024 00:23:49 -0600</pubDate>
	<link>https://bioinformaticsonline.com/bookmarks/view/44479/doubletrouble-identify-duplicated-genes-from-whole-genome-protein-sequences-and-classify</link>
	<title><![CDATA[doubletrouble: identify duplicated genes from whole-genome protein sequences and classify]]></title>
	<description><![CDATA[<p><span>doubletrouble aims to identify duplicated genes from whole-genome protein sequences and classify them based on their modes of duplication. The duplication modes are i. segmental duplication (SD); ii. tandem duplication (TD); iii. proximal duplication (PD); iv. transposed duplication (TRD) and; v. dispersed duplication (DD). Transposon-derived duplicates (TRD) can be further subdivided into rTRD (retrotransposon-derived duplication) and dTRD (DNA transposon-derived duplication). If users want a simpler classification scheme, duplicates can also be classified into SD- and SSD-derived (small-scale duplication) gene pairs. Besides classifying gene pairs, users can also classify genes, so that each gene is assigned a unique mode of duplication. Users can also calculate substitution rates per substitution site (i.e., Ka and Ks) from duplicate pairs, find peaks in Ks distributions with Gaussian Mixture Models (GMMs), and classify gene pairs into age groups based on Ks peaks.</span></p><p>Address of the bookmark: <a href="https://bioconductor.org/packages/release/bioc/html/doubletrouble.html" rel="nofollow">https://bioconductor.org/packages/release/bioc/html/doubletrouble.html</a></p>]]></description>
	<dc:creator>LEGE</dc:creator>
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