Difference between revisions of "Part:BBa K1321339"

 
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__NOTOC__
 
__NOTOC__
 
<partinfo>BBa_K1321339 short</partinfo>
 
<partinfo>BBa_K1321339 short</partinfo>
  
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CBDcenA in Freiburg format (RFC 25).
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Cellulose binding domain of Endoglucanase A (cenA) from ''Cellulomonas fimi'' with an endogenous C-terminal linker. The part is in Freiburg format (RFC 25) for ease of use in protein fusions.  
  
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<!-- Add more about the biology of this part here
 
 
===Usage and Biology===
 
===Usage and Biology===
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The cellulose binding domain region occurs at the N-terminus of the cenA gene ([http://www.uniprot.org/uniprot/P07984 UniProt P07984]) and is from the [http://www.cazy.org/CBM2.html CBM family 2].
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The linker sequence (PTTSPTPTPTPTTPTPTPTPTPTPTPTVTP) is Pro-Thr box which has an extended conformation and acts as a hinge region [1]. The endoglucanase CBDCenA has 50% homology to the exoglucanase CBDcex (BBa_K863101) and the linker is highly conserved in both, but the order of the catalytic, linker and cellulose-binding regions is reversed [2]. It has been shown that CBDCenA has the highest binding affinity for crystalline cellulose out of the ''C. fimi'' CBDs [3].
  
 
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<span class='h3bb'>Sequence and Features</span>
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===Sequence and Features===
 
<partinfo>BBa_K1321339 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K1321339 SequenceAndFeatures</partinfo>
  
  
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<!-- Uncomment this to enable Functional Parameter display
 
 
===Functional Parameters===
 
===Functional Parameters===
 
<partinfo>BBa_K1321339 parameters</partinfo>
 
<partinfo>BBa_K1321339 parameters</partinfo>
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<html><!--- Please copy this table containing parameters for BBa_ at the end of the parametrs section ahead of the references. ---><style type="text/css">table#AutoAnnotator {border:1px solid black; width:100%; border-collapse:collapse;} th#AutoAnnotatorHeader { border:1px solid black; width:100%; background-color: rgb(221, 221, 221);} td.AutoAnnotator1col { width:100%; border:1px solid black; } span.AutoAnnotatorSequence { font-family:'Courier New', Arial; } td.AutoAnnotatorSeqNum { text-align:right; width:2%; } td.AutoAnnotatorSeqSeq { width:98% } td.AutoAnnotatorSeqFeat1 { width:3% } td.AutoAnnotatorSeqFeat2a { width:27% } td.AutoAnnotatorSeqFeat2b { width:97% } td.AutoAnnotatorSeqFeat3 { width:70% } table.AutoAnnotatorNoBorder { border:0px; width:100%; border-collapse:collapse; } table.AutoAnnotatorWithBorder { border:1px solid black; width:100%; border-collapse:collapse; } td.AutoAnnotatorOuterAmino { border:0px solid black; width:20% } td.AutoAnnotatorInnerAmino { border:1px solid black; width:50% } td.AutoAnnotatorAminoCountingOuter { border:1px solid black; width:40%;  } td.AutoAnnotatorBiochemParOuter { border:1px solid black; width:60%; } td.AutoAnnotatorAminoCountingInner1 { width: 7.5% } td.AutoAnnotatorAminoCountingInner2 { width:62.5% } td.AutoAnnotatorAminoCountingInner3 { width:30% } td.AutoAnnotatorBiochemParInner1 { width: 5% } td.AutoAnnotatorBiochemParInner2 { width:55% } td.AutoAnnotatorBiochemParInner3 { width:40% } td.AutoAnnotatorCodonUsage1 { width: 3% } td.AutoAnnotatorCodonUsage2 { width:14.2% } td.AutoAnnotatorCodonUsage3 { width:13.8% } td.AutoAnnotatorAlignment1 { width: 3% } td.AutoAnnotatorAlignment2 { width: 10% } td.AutoAnnotatorAlignment3 { width: 87% } td.AutoAnnotatorLocalizationOuter {border:1px solid black; width:40%} td.AutoAnnotatorGOOuter {border:1px solid black; width:60%} td.AutoAnnotatorLocalization1 { width: 7.5% } td.AutoAnnotatorLocalization2 { width: 22.5% } td.AutoAnnotatorLocalization3 { width: 70% } td.AutoAnnotatorGO1 { width: 5% } td.AutoAnnotatorGO2 { width: 35% } td.AutoAnnotatorGO3 { width: 60% } td.AutoAnnotatorPredFeat1 { width:3% } td.AutoAnnotatorPredFeat2a { width:27% } td.AutoAnnotatorPredFeat3 { width:70% } div.AutoAnnotator_trans { position:absolute; background:rgb(11,140,143); background-color:rgba(11,140,143, 0.8); height:5px; top:100px; } div.AutoAnnotator_sec_helix { position:absolute; background:rgb(102,0,102); background-color:rgba(102,0,102, 0.8); height:5px; top:110px; } div.AutoAnnotator_sec_strand { position:absolute; background:rgb(245,170,26); background-color:rgba(245,170,26, 1); height:5px; top:110px; } div.AutoAnnotator_acc_buried { position:absolute; background:rgb(89,168,15); background-color:rgba(89,168,15, 0.8); height:5px; top:120px; } div.AutoAnnotator_acc_exposed { position:absolute; background:rgb(0, 0, 255); background-color:rgba(0, 0, 255, 0.8); height:5px; top:120px; } div.AutoAnnotator_dis { position:absolute; text-align:center; font-family:Arial,Helvetica,sans-serif; background:rgb(255, 200, 0); background-color:rgba(255, 200, 0, 1); height:16px; width:16px; top:80px; border-radius:50%; } </style><div id='AutoAnnotator_container_1413204433653'><table id="AutoAnnotator"><tr><!-- Time stamp in ms since 1/1/1970 1413204433653 --><th id="AutoAnnotatorHeader" colspan="2">Protein data table for BioBrick <a href="https://parts.igem.org/wiki/index.php?title=Part:BBa_K1321339">BBa_K1321339</a> automatically created by the <a href="http://2013.igem.org/Team:TU-Munich/Results/AutoAnnotator">BioBrick-AutoAnnotator</a> version 1.0</th></tr><tr><td class="AutoAnnotator1col" colspan="2"><strong>Nucleotide sequence</strong> in <strong>RFC 25</strong>: (underlined part encodes the protein)<br><span class="AutoAnnotatorSequence">&nbsp;<u>ATGGCCGGC&nbsp;...&nbsp;CCCACCGGT</u>TAA</span><br>&nbsp;<strong>ORF</strong> from nucleotide position 1 to 423 (excluding stop-codon)</td></tr><tr><td class="AutoAnnotator1col" colspan="2"><strong>Amino acid sequence:</strong> (RFC 25 scars in shown in bold, other sequence features underlined; both given below)<br><span class="AutoAnnotatorSequence"><table class="AutoAnnotatorNoBorder"><tr><td class="AutoAnnotatorSeqNum">1&nbsp;<br>101&nbsp;</td><td class="AutoAnnotatorSeqSeq">MAGAPGCRVDYAVTNQWPGGFGANVTITNLGDPVSSWKLDWTYTAGQRIQQLWNGTASTNGGQVSVTSLPWNGSIPTGGTASFGFNGSWAGSNPTPASFS<br>LNGTTCTGTPTTSPTPTPTPTTPTPTPTPTPTPTPTVTPTG*</td></tr></table></span></td></tr><tr><td class="AutoAnnotator1col" colspan="2"><strong>Sequence features:</strong> (with their position in the amino acid sequence, see the <a href="http://2013.igem.org/Team:TU-Munich/Results/Software/FeatureList">list of supported features</a>)<table class="AutoAnnotatorNoBorder"><tr><td class="AutoAnnotatorSeqFeat1"></td><td class="AutoAnnotatorSeqFeat2b">None of the supported features appeared in the sequence</td></tr></table></td></tr><tr><td class="AutoAnnotator1col" colspan="2"><strong>Amino acid composition:</strong><table class="AutoAnnotatorNoBorder"><tr><td class="AutoAnnotatorOuterAmino"><table class="AutoAnnotatorWithBorder"><tr><td class="AutoAnnotatorInnerAmino">Ala (A)</td><td class="AutoAnnotatorInnerAmino">9 (6.4%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Arg (R)</td><td class="AutoAnnotatorInnerAmino">2 (1.4%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Asn (N)</td><td class="AutoAnnotatorInnerAmino">9 (6.4%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Asp (D)</td><td class="AutoAnnotatorInnerAmino">3 (2.1%)</td></tr></table></td><td class="AutoAnnotatorOuterAmino"><table class="AutoAnnotatorWithBorder"><tr><td class="AutoAnnotatorInnerAmino">Cys (C)</td><td class="AutoAnnotatorInnerAmino">2 (1.4%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Gln (Q)</td><td class="AutoAnnotatorInnerAmino">5 (3.5%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Glu (E)</td><td class="AutoAnnotatorInnerAmino">0 (0.0%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Gly (G)</td><td class="AutoAnnotatorInnerAmino">19 (13.5%)</td></tr></table></td><td class="AutoAnnotatorOuterAmino"><table class="AutoAnnotatorWithBorder"><tr><td class="AutoAnnotatorInnerAmino">His (H)</td><td class="AutoAnnotatorInnerAmino">0 (0.0%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Ile (I)</td><td class="AutoAnnotatorInnerAmino">3 (2.1%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Leu (L)</td><td class="AutoAnnotatorInnerAmino">5 (3.5%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Lys (K)</td><td class="AutoAnnotatorInnerAmino">1 (0.7%)</td></tr></table></td><td class="AutoAnnotatorOuterAmino"><table class="AutoAnnotatorWithBorder"><tr><td class="AutoAnnotatorInnerAmino">Met (M)</td><td class="AutoAnnotatorInnerAmino">1 (0.7%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Phe (F)</td><td class="AutoAnnotatorInnerAmino">4 (2.8%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Pro (P)</td><td class="AutoAnnotatorInnerAmino">20 (14.2%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Ser (S)</td><td class="AutoAnnotatorInnerAmino">12 (8.5%)</td></tr></table></td><td class="AutoAnnotatorOuterAmino"><table class="AutoAnnotatorWithBorder"><tr><td class="AutoAnnotatorInnerAmino">Thr (T)</td><td class="AutoAnnotatorInnerAmino">31 (22.0%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Trp (W)</td><td class="AutoAnnotatorInnerAmino">6 (4.3%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Tyr (Y)</td><td class="AutoAnnotatorInnerAmino">2 (1.4%)</td></tr><tr><td class="AutoAnnotatorInnerAmino">Val (V)</td><td class="AutoAnnotatorInnerAmino">7 (5.0%)</td></tr></table></td></tr></table></td></tr><tr><td class="AutoAnnotatorAminoCountingOuter"><strong>Amino acid counting</strong><table class="AutoAnnotatorNoBorder"><tr><td class="AutoAnnotatorAminoCountingInner1"></td><td class="AutoAnnotatorAminoCountingInner2">Total number:</td><td class="AutoAnnotatorAminoCountingInner3">141</td></tr><tr><td class="AutoAnnotatorAminoCountingInner1"></td><td class="AutoAnnotatorAminoCountingInner2">Positively charged (Arg+Lys):</td><td class="AutoAnnotatorAminoCountingInner3">3 (2.1%)</td></tr><tr><td class="AutoAnnotatorAminoCountingInner1"></td><td class="AutoAnnotatorAminoCountingInner2">Negatively charged (Asp+Glu):</td><td class="AutoAnnotatorAminoCountingInner3">3 (2.1%)</td></tr><tr><td class="AutoAnnotatorAminoCountingInner1"></td><td class="AutoAnnotatorAminoCountingInner2">Aromatic (Phe+His+Try+Tyr):</td><td class="AutoAnnotatorAminoCountingInner3">12 (8.5%)</td></tr></table></td><td class="AutoAnnotatorBiochemParOuter"><strong>Biochemical parameters</strong><table class="AutoAnnotatorNoBorder"><tr><td class="AutoAnnotatorBiochemParInner1"></td><td class="AutoAnnotatorBiochemParInner2">Atomic composition:</td><td class="AutoAnnotatorBiochemParInner3">C<sub>630</sub>H<sub>950</sub>N<sub>168</sub>O<sub>207</sub>S<sub>3</sub></td></tr><tr><td class="AutoAnnotatorBiochemParInner1"></td><td class="AutoAnnotatorBiochemParInner2">Molecular mass [Da]:</td><td class="AutoAnnotatorBiochemParInner3">14285.7</td></tr><tr><td class="AutoAnnotatorBiochemParInner1"></td><td class="AutoAnnotatorBiochemParInner2">Theoretical pI:</td><td class="AutoAnnotatorBiochemParInner3">5.79</td></tr><tr><td class="AutoAnnotatorBiochemParInner1"></td><td class="AutoAnnotatorBiochemParInner2">Extinction coefficient at 280 nm [M<sup>-1</sup> cm<sup>-1</sup>]:</td><td class="AutoAnnotatorBiochemParInner3">35980 / 36105 (all Cys red/ox)</td></tr></table></td></tr><tr><td class="AutoAnnotator1col" colspan="2"><strong>Plot for hydrophobicity, charge, predicted secondary structure, solvent accessability, transmembrane helices and disulfid bridges</strong>&nbsp;<input type='button' id='hydrophobicity_charge_button' onclick='show_or_hide_plot_1413204433653()' value='Show'><span id="hydrophobicity_charge_explanation"></span><div id="hydrophobicity_charge_container" style='display:none'><div id="hydrophobicity_charge_placeholder0" style="width:100%;height:150px"></div></div></td></tr><tr><td class="AutoAnnotator1col" colspan="2"><strong>Codon usage</strong><table class="AutoAnnotatorNoBorder"><tr><td class="AutoAnnotatorCodonUsage1"></td><td class="AutoAnnotatorCodonUsage2">Organism:</td><td class="AutoAnnotatorCodonUsage3"><i>E. coli</i></td><td class="AutoAnnotatorCodonUsage3"><i>B. subtilis</i></td><td class="AutoAnnotatorCodonUsage3"><i>S. cerevisiae</i></td><td class="AutoAnnotatorCodonUsage3"><i>A. thaliana</i></td><td class="AutoAnnotatorCodonUsage3"><i>P. patens</i></td><td class="AutoAnnotatorCodonUsage3">Mammals</td></tr><tr><td class="AutoAnnotatorCodonUsage1"></td><td class="AutoAnnotatorCodonUsage2">Codon quality (<a href="http://en.wikipedia.org/wiki/Codon_Adaptation_Index">CAI</a>):</td><td class="AutoAnnotatorCodonUsage3">excellent (0.85)</td><td class="AutoAnnotatorCodonUsage3">good (0.67)</td><td class="AutoAnnotatorCodonUsage3">good (0.60)</td><td class="AutoAnnotatorCodonUsage3">good (0.67)</td><td class="AutoAnnotatorCodonUsage3">excellent (0.82)</td><td class="AutoAnnotatorCodonUsage3">good (0.64)</td></tr></table></td></tr><tr><td class="AutoAnnotator1col" colspan="2"><strong>Alignments</strong> (obtained from <a href='http://predictprotein.org'>PredictProtein.org</a>)<br>&nbsp;&nbsp;&nbsp;There were no alignments for this protein in the data base. The BLAST search was initialized and should be ready in a few hours.</td></tr><tr><th id='AutoAnnotatorHeader' colspan="2"><strong>Predictions</strong> (obtained from <a href='http://predictprotein.org'>PredictProtein.org</a>)</th></tr><tr><td class="AutoAnnotator1col" colspan="2">&nbsp;&nbsp;&nbsp;There were no predictions for this protein in the data base. The prediction was initialized and should be ready in a few hours.</td><tr><td class="AutoAnnotator1col" colspan="2"> The BioBrick-AutoAnnotator was created by <a href="http://2013.igem.org/Team:TU-Munich">TU-Munich 2013</a> iGEM team. For more information please see the <a href="http://2013.igem.org/Team:TU-Munich/Results/Software">documentation</a>.<br>If you have any questions, comments or suggestions, please leave us a <a href="http://2013.igem.org/Team:TU-Munich/Results/AutoAnnotator">comment</a>.</td></tr></table></div><br><!-- IMPORTANT: DON'T REMOVE THIS LINE, OTHERWISE NOT SUPPORTED FOR IE BEFORE 9 --><!--[if lte IE 8]><script language="javascript" type="text/javascript" src="http://2013.igem.org/Team:TU-Munich/excanvas.js"></script><![endif]--><script type='text/javascript' src='http://code.jquery.com/jquery-1.10.0.min.js'></script><script type='text/javascript' src='http://2013.igem.org/Team:TU-Munich/Flot.js?action=raw&ctype=text/js'></script><script>var jqAutoAnnotator = jQuery.noConflict(true);function show_or_hide_plot_1413204433653(){hydrophobicity_datapoints = [[2.5,0.70],[3.5,0.24],[4.5,0.38],[5.5,-0.44],[6.5,0.04],[7.5,-0.34],[8.5,-0.52],[9.5,-0.66],[10.5,1.08],[11.5,0.10],[12.5,0.10],[13.5,-0.34],[14.5,-0.88],[15.5,-2.04],[16.5,-1.98],[17.5,-1.36],[18.5,-0.10],[19.5,-0.00],[20.5,0.68],[21.5,0.06],[22.5,0.98],[23.5,0.28],[24.5,1.26],[25.5,0.76],[26.5,0.76],[27.5,0.68],[28.5,0.74],[29.5,-0.86],[30.5,-1.04],[31.5,0.50],[32.5,-0.42],[33.5,-0.50],[34.5,0.02],[35.5,-0.44],[36.5,-0.52],[37.5,-1.06],[38.5,-1.08],[39.5,-1.04],[40.5,-0.52],[41.5,-1.42],[42.5,-0.36],[43.5,-0.26],[44.5,-0.82],[45.5,-1.46],[46.5,-0.42],[47.5,-1.48],[48.5,-2.10],[49.5,-0.64],[50.5,0.08],[51.5,-1.52],[52.5,-0.90],[53.5,-0.34],[54.5,-0.74],[55.5,-0.72],[56.5,-0.16],[57.5,-0.78],[58.5,-0.72],[59.5,-1.16],[60.5,-1.70],[61.5,-0.72],[62.5,-0.18],[63.5,0.74],[64.5,0.68],[65.5,1.22],[66.5,1.14],[67.5,0.98],[68.5,-0.04],[69.5,-0.60],[70.5,-0.52],[71.5,-1.44],[72.5,-0.22],[73.5,-0.36],[74.5,0.20],[75.5,0.20],[76.5,0.28],[77.5,-0.76],[78.5,-0.08],[79.5,-0.10],[80.5,0.54],[81.5,0.54],[82.5,1.24],[83.5,0.18],[84.5,0.26],[85.5,-0.46],[86.5,-0.56],[87.5,-0.76],[88.5,-0.14],[89.5,-0.22],[90.5,-0.76],[91.5,-0.90],[92.5,-1.40],[93.5,-1.64],[94.5,-1.12],[95.5,-0.58],[96.5,0.30],[97.5,0.28],[98.5,1.36],[99.5,0.30],[100.5,0.38],[101.5,-0.32],[102.5,-0.30],[103.5,-0.56],[104.5,-0.00],[105.5,-0.00],[106.5,-0.00],[107.5,-0.18],[108.5,-0.82],[109.5,-0.82],[110.5,-0.90],[111.5,-1.08],[112.5,-0.90],[113.5,-1.08],[114.5,-1.08],[115.5,-1.24],[116.5,-1.06],[117.5,-1.24],[118.5,-1.06],[119.5,-1.06],[120.5,-1.06],[121.5,-1.06],[122.5,-1.06],[123.5,-1.06],[124.5,-1.24],[125.5,-1.06],[126.5,-1.24],[127.5,-1.06],[128.5,-1.24],[129.5,-1.06],[130.5,-1.24],[131.5,-1.06],[132.5,-1.24],[133.5,-1.06],[134.5,-0.08],[135.5,0.10],[136.5,-0.08],[137.5,0.10],[138.5,0.16]];charge_datapoints = [[2.5,0.00],[3.5,0.00],[4.5,0.00],[5.5,0.20],[6.5,0.20],[7.5,0.00],[8.5,0.00],[9.5,0.00],[10.5,-0.20],[11.5,-0.20],[12.5,0.00],[13.5,0.00],[14.5,0.00],[15.5,0.00],[16.5,0.00],[17.5,0.00],[18.5,0.00],[19.5,0.00],[20.5,0.00],[21.5,0.00],[22.5,0.00],[23.5,0.00],[24.5,0.00],[25.5,0.00],[26.5,0.00],[27.5,0.00],[28.5,0.00],[29.5,-0.20],[30.5,-0.20],[31.5,-0.20],[32.5,-0.20],[33.5,-0.20],[34.5,0.00],[35.5,0.20],[36.5,0.20],[37.5,0.00],[38.5,0.00],[39.5,0.00],[40.5,-0.20],[41.5,-0.20],[42.5,0.00],[43.5,0.00],[44.5,0.00],[45.5,0.20],[46.5,0.20],[47.5,0.20],[48.5,0.20],[49.5,0.20],[50.5,0.00],[51.5,0.00],[52.5,0.00],[53.5,0.00],[54.5,0.00],[55.5,0.00],[56.5,0.00],[57.5,0.00],[58.5,0.00],[59.5,0.00],[60.5,0.00],[61.5,0.00],[62.5,0.00],[63.5,0.00],[64.5,0.00],[65.5,0.00],[66.5,0.00],[67.5,0.00],[68.5,0.00],[69.5,0.00],[70.5,0.00],[71.5,0.00],[72.5,0.00],[73.5,0.00],[74.5,0.00],[75.5,0.00],[76.5,0.00],[77.5,0.00],[78.5,0.00],[79.5,0.00],[80.5,0.00],[81.5,0.00],[82.5,0.00],[83.5,0.00],[84.5,0.00],[85.5,0.00],[86.5,0.00],[87.5,0.00],[88.5,0.00],[89.5,0.00],[90.5,0.00],[91.5,0.00],[92.5,0.00],[93.5,0.00],[94.5,0.00],[95.5,0.00],[96.5,0.00],[97.5,0.00],[98.5,0.00],[99.5,0.00],[100.5,0.00],[101.5,0.00],[102.5,0.00],[103.5,0.00],[104.5,0.00],[105.5,0.00],[106.5,0.00],[107.5,0.00],[108.5,0.00],[109.5,0.00],[110.5,0.00],[111.5,0.00],[112.5,0.00],[113.5,0.00],[114.5,0.00],[115.5,0.00],[116.5,0.00],[117.5,0.00],[118.5,0.00],[119.5,0.00],[120.5,0.00],[121.5,0.00],[122.5,0.00],[123.5,0.00],[124.5,0.00],[125.5,0.00],[126.5,0.00],[127.5,0.00],[128.5,0.00],[129.5,0.00],[130.5,0.00],[131.5,0.00],[132.5,0.00],[133.5,0.00],[134.5,0.00],[135.5,0.00],[136.5,0.00],[137.5,0.00],[138.5,0.00]];dis_datapoints 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id=\'acc_checkbox\' checked=\'checked\'>&nbsp;Predicted solvent accessability: Exposed (<img src=\'https://static.igem.org/mediawiki/2013/1/16/TUM13_exposed_icon.png\' alt=\'blue bars\' height=\'10\'></img>) and buried (<img src=\'https://static.igem.org/mediawiki/2013/0/0b/TUM13_buried_icon.png\' alt=\'green bars\' height=\'10\'></img>) residues';description_html = description_html + '<br></div>';jqAutoAnnotator('#AutoAnnotator_container_1413204433653 #hydrophobicity_charge_explanation').html(description_html);plot_according_to_selectors_1413204433653();jqAutoAnnotator('#AutoAnnotator_container_1413204433653 #AutoAnnotator_plot_selectors').find('input').click(plot_according_to_selectors_1413204433653);}else{jqAutoAnnotator('#AutoAnnotator_container_1413204433653 #hydrophobicity_charge_container').css('display','none');jqAutoAnnotator('#AutoAnnotator_container_1413204433653 #hydrophobicity_charge_button').val('Show');jqAutoAnnotator('#AutoAnnotator_container_1413204433653 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 +
 
 +
===References===
 +
1. Gilkes, N.R. et al., 1989. Structural and functional analysis of a bacterial cellulase by proteolysis. The Journal of biological chemistry, 264(30), pp.17802–8. Available at: http://www.ncbi.nlm.nih.gov/pubmed/2681184
 +
 
 +
2. Warren, R.A. et al., 1986. Sequence conservation and region shuffling in an endoglucanase and an exoglucanase from Cellulomonas fimi. Proteins, 1(4), pp.335–41. Available at: http://www.ncbi.nlm.nih.gov/pubmed/3130625
 +
 
 +
3. Kim, H.-D. et al., 2013. Enzyme-linked assay of cellulose-binding domain functions from Cellulomonas fimi on multi-well microtiter plate. Biotechnology and Bioprocess Engineering, 18(3), pp.575–580. Available at: http://link.springer.com/10.1007/s12257-013-0242-3

Revision as of 12:59, 13 October 2014

CBDcenA+Linker, RFC 25 standard

Cellulose binding domain of Endoglucanase A (cenA) from Cellulomonas fimi with an endogenous C-terminal linker. The part is in Freiburg format (RFC 25) for ease of use in protein fusions.

Usage and Biology

The cellulose binding domain region occurs at the N-terminus of the cenA gene ([http://www.uniprot.org/uniprot/P07984 UniProt P07984]) and is from the [http://www.cazy.org/CBM2.html CBM family 2].

The linker sequence (PTTSPTPTPTPTTPTPTPTPTPTPTPTVTP) is Pro-Thr box which has an extended conformation and acts as a hinge region [1]. The endoglucanase CBDCenA has 50% homology to the exoglucanase CBDcex (BBa_K863101) and the linker is highly conserved in both, but the order of the catalytic, linker and cellulose-binding regions is reversed [2]. It has been shown that CBDCenA has the highest binding affinity for crystalline cellulose out of the C. fimi CBDs [3].

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Functional Parameters

Protein data table for BioBrick BBa_K1321339 automatically created by the BioBrick-AutoAnnotator version 1.0
Nucleotide sequence in RFC 25: (underlined part encodes the protein)
 ATGGCCGGC ... CCCACCGGTTAA
 ORF from nucleotide position 1 to 423 (excluding stop-codon)
Amino acid sequence: (RFC 25 scars in shown in bold, other sequence features underlined; both given below)
1 
101 		MAGAPGCRVDYAVTNQWPGGFGANVTITNLGDPVSSWKLDWTYTAGQRIQQLWNGTASTNGGQVSVTSLPWNGSIPTGGTASFGFNGSWAGSNPTPASFS
LNGTTCTGTPTTSPTPTPTPTTPTPTPTPTPTPTPTVTPTG*
Sequence features: (with their position in the amino acid sequence, see the list of supported features)
None of the supported features appeared in the sequence
Amino acid composition:
Ala (A)9 (6.4%)
Arg (R)2 (1.4%)
Asn (N)9 (6.4%)
Asp (D)3 (2.1%)
Cys (C)2 (1.4%)
Gln (Q)5 (3.5%)
Glu (E)0 (0.0%)
Gly (G)19 (13.5%)
His (H)0 (0.0%)
Ile (I)3 (2.1%)
Leu (L)5 (3.5%)
Lys (K)1 (0.7%)
Met (M)1 (0.7%)
Phe (F)4 (2.8%)
Pro (P)20 (14.2%)
Ser (S)12 (8.5%)
Thr (T)31 (22.0%)
Trp (W)6 (4.3%)
Tyr (Y)2 (1.4%)
Val (V)7 (5.0%)
Amino acid counting
Total number:141
Positively charged (Arg+Lys):3 (2.1%)
Negatively charged (Asp+Glu):3 (2.1%)
Aromatic (Phe+His+Try+Tyr):12 (8.5%)
Biochemical parameters
Atomic composition:C630H950N168O207S3
Molecular mass [Da]:14285.7
Theoretical pI:5.79
Extinction coefficient at 280 nm [M-1 cm-1]:35980 / 36105 (all Cys red/ox)
Plot for hydrophobicity, charge, predicted secondary structure, solvent accessability, transmembrane helices and disulfid bridges 
Codon usage
Organism:E. coliB. subtilisS. cerevisiaeA. thalianaP. patensMammals
Codon quality (CAI):excellent (0.85)good (0.67)good (0.60)good (0.67)excellent (0.82)good (0.64)
Alignments (obtained from PredictProtein.org)
   There were no alignments for this protein in the data base. The BLAST search was initialized and should be ready in a few hours.
Predictions (obtained from PredictProtein.org)
   There were no predictions for this protein in the data base. The prediction was initialized and should be ready in a few hours.
The BioBrick-AutoAnnotator was created by TU-Munich 2013 iGEM team. For more information please see the documentation.
If you have any questions, comments or suggestions, please leave us a comment.

References

1. Gilkes, N.R. et al., 1989. Structural and functional analysis of a bacterial cellulase by proteolysis. The Journal of biological chemistry, 264(30), pp.17802–8. Available at: http://www.ncbi.nlm.nih.gov/pubmed/2681184

2. Warren, R.A. et al., 1986. Sequence conservation and region shuffling in an endoglucanase and an exoglucanase from Cellulomonas fimi. Proteins, 1(4), pp.335–41. Available at: http://www.ncbi.nlm.nih.gov/pubmed/3130625

3. Kim, H.-D. et al., 2013. Enzyme-linked assay of cellulose-binding domain functions from Cellulomonas fimi on multi-well microtiter plate. Biotechnology and Bioprocess Engineering, 18(3), pp.575–580. Available at: http://link.springer.com/10.1007/s12257-013-0242-3