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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Comparative genomics reveals high biological diversity and specific adaptations in the industrially and medically important fungal genus <italic>Aspergillus</italic></title><author><name sortKey="De Vries, Ronald P" sort="De Vries, Ronald P" uniqKey="De Vries R" first="Ronald P." last="De Vries">Ronald P. De Vries</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000000120346234</institution-id><institution-id institution-id-type="GRID">grid.5477.1</institution-id><institution>Fungal Molecular Physiology,</institution><institution>Utrecht University,</institution></institution-wrap>Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Riley, Robert" sort="Riley, Robert" uniqKey="Riley R" first="Robert" last="Riley">Robert Riley</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Wiebenga, Ad" sort="Wiebenga, Ad" uniqKey="Wiebenga A" first="Ad" last="Wiebenga">Ad Wiebenga</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000000120346234</institution-id><institution-id institution-id-type="GRID">grid.5477.1</institution-id><institution>Fungal Molecular Physiology,</institution><institution>Utrecht University,</institution></institution-wrap>Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Aguilar Osorio, Guillermo" sort="Aguilar Osorio, Guillermo" uniqKey="Aguilar Osorio G" first="Guillermo" last="Aguilar-Osorio">Guillermo Aguilar-Osorio</name><affiliation><nlm:aff id="Aff4"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2159 0001</institution-id><institution-id institution-id-type="GRID">grid.9486.3</institution-id><institution>Department of Food Science and Biotechnology, Faculty of Chemistry,</institution><institution>National University of Mexico,</institution></institution-wrap>Ciudad Universitaria, D.F. C.P. 04510 Mexico</nlm:aff></affiliation></author><author><name sortKey="Amillis, Sotiris" sort="Amillis, Sotiris" uniqKey="Amillis S" first="Sotiris" last="Amillis">Sotiris Amillis</name><affiliation><nlm:aff id="Aff5"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2155 0800</institution-id><institution-id institution-id-type="GRID">grid.5216.0</institution-id><institution>Department of Biology,</institution><institution>National and Kapodistrian University of Athens,</institution></institution-wrap>Panepistimioupolis, 15781 Athens, Greece</nlm:aff></affiliation></author><author><name sortKey="Uchima, Cristiane Akemi" sort="Uchima, Cristiane Akemi" uniqKey="Uchima C" first="Cristiane Akemi" last="Uchima">Cristiane Akemi Uchima</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation><affiliation><nlm:aff id="Aff60">Present address: VTT Brasil, Alameda Inajá, 123, CEP 06460-055 Barueri, São Paulo Brazil</nlm:aff></affiliation></author><author><name sortKey="Anderluh, Gregor" sort="Anderluh, Gregor" uniqKey="Anderluh G" first="Gregor" last="Anderluh">Gregor Anderluh</name><affiliation><nlm:aff id="Aff7"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0661 0844</institution-id><institution-id institution-id-type="GRID">grid.454324.0</institution-id><institution>Laboratory for Molecular Biology and Nanobiotechnology,</institution><institution>National Institute of Chemistry,</institution></institution-wrap>Hajdrihova 19, 1000 Ljubljana, Slovenia</nlm:aff></affiliation></author><author><name sortKey="Asadollahi, Mojtaba" sort="Asadollahi, Mojtaba" uniqKey="Asadollahi M" first="Mojtaba" last="Asadollahi">Mojtaba Asadollahi</name><affiliation><nlm:aff id="Aff8"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biochemical Engineering, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Askin, Marion" sort="Askin, Marion" uniqKey="Askin M" first="Marion" last="Askin">Marion Askin</name><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff61"><institution-wrap><institution-id institution-id-type="GRID">grid.431777.1</institution-id><institution></institution><institution>Present address: CSIRO Publishing,</institution></institution-wrap>Unipark, Building 1 Level 1, 195 Wellington Road, Clayton, VIC 3168 Australia</nlm:aff></affiliation></author><author><name sortKey="Barry, Kerrie" sort="Barry, Kerrie" uniqKey="Barry K" first="Kerrie" last="Barry">Kerrie Barry</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Battaglia, Evy" sort="Battaglia, Evy" uniqKey="Battaglia E" first="Evy" last="Battaglia">Evy Battaglia</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000000120346234</institution-id><institution-id institution-id-type="GRID">grid.5477.1</institution-id><institution>Fungal Molecular Physiology,</institution><institution>Utrecht University,</institution></institution-wrap>Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Bayram, Ozgur" sort="Bayram, Ozgur" uniqKey="Bayram O" first="Özgür" last="Bayram">Özgür Bayram</name><affiliation><nlm:aff id="Aff10"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2364 4210</institution-id><institution-id institution-id-type="GRID">grid.7450.6</institution-id><institution>Department of Molecular Microbiology and Genetics,</institution><institution>Institute for Microbiology and Genetics, Georg August University Göttingen,</institution></institution-wrap>Grisebachstr. 8, 37077 Göttingen, Germany</nlm:aff></affiliation><affiliation><nlm:aff id="Aff11"><institution-wrap><institution-id institution-id-type="ISNI">0000 0000 9331 9029</institution-id><institution-id institution-id-type="GRID">grid.95004.38</institution-id><institution>Department of Biology,</institution><institution>Maynooth University,</institution></institution-wrap>Maynooth, Co. Kildare Ireland</nlm:aff></affiliation></author><author><name sortKey="Benocci, Tiziano" sort="Benocci, Tiziano" uniqKey="Benocci T" first="Tiziano" last="Benocci">Tiziano Benocci</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000000120346234</institution-id><institution-id institution-id-type="GRID">grid.5477.1</institution-id><institution>Fungal Molecular Physiology,</institution><institution>Utrecht University,</institution></institution-wrap>Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Braus Stromeyer, Susanna A" sort="Braus Stromeyer, Susanna A" uniqKey="Braus Stromeyer S" first="Susanna A." last="Braus-Stromeyer">Susanna A. Braus-Stromeyer</name><affiliation><nlm:aff id="Aff10"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2364 4210</institution-id><institution-id institution-id-type="GRID">grid.7450.6</institution-id><institution>Department of Molecular Microbiology and Genetics,</institution><institution>Institute for Microbiology and Genetics, Georg August University Göttingen,</institution></institution-wrap>Grisebachstr. 8, 37077 Göttingen, Germany</nlm:aff></affiliation></author><author><name sortKey="Caldana, Camila" sort="Caldana, Camila" uniqKey="Caldana C" first="Camila" last="Caldana">Camila Caldana</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation><affiliation><nlm:aff id="Aff12">Max Planck Partner Group, Brazilian Bioethanol Science and Technology Laboratory, CEP 13083-100 Campinas, Sao Paulo Brazil</nlm:aff></affiliation></author><author><name sortKey="Canovas, David" sort="Canovas, David" uniqKey="Canovas D" first="David" last="Cánovas">David Cánovas</name><affiliation><nlm:aff id="Aff13"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2168 1229</institution-id><institution-id institution-id-type="GRID">grid.9224.d</institution-id><institution>Department of Genetics, Faculty of Biology,</institution><institution>University of Seville,</institution></institution-wrap>Avda de Reina Mercedes 6, 41012 Sevilla, Spain</nlm:aff></affiliation><affiliation><nlm:aff id="Aff14"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2298 5320</institution-id><institution-id institution-id-type="GRID">grid.5173.0</institution-id><institution>Fungal Genetics and Genomics Unit, Department of Applied Genetics and Cell Biology,</institution><institution>University of Natural Resources and Life Sciences (BOKU) Vienna,</institution></institution-wrap>Vienna, Austria</nlm:aff></affiliation></author><author><name sortKey="Cerqueira, Gustavo C" sort="Cerqueira, Gustavo C" uniqKey="Cerqueira G" first="Gustavo C." last="Cerqueira">Gustavo C. Cerqueira</name><affiliation><nlm:aff id="Aff15"><institution-wrap><institution-id institution-id-type="GRID">grid.66859.34</institution-id><institution></institution><institution>Broad Institute of Harvard and MIT,</institution></institution-wrap>75 Ames St, Cambridge, MA 02142 USA</nlm:aff></affiliation></author><author><name sortKey="Chen, Fusheng" sort="Chen, Fusheng" uniqKey="Chen F" first="Fusheng" last="Chen">Fusheng Chen</name><affiliation><nlm:aff id="Aff16"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1790 4137</institution-id><institution-id institution-id-type="GRID">grid.35155.37</institution-id><institution>College of Food Science and Technology,</institution><institution>Huazhong Agricultural University,</institution></institution-wrap>Wuhan, 430070 China</nlm:aff></affiliation></author><author><name sortKey="Chen, Wanping" sort="Chen, Wanping" uniqKey="Chen W" first="Wanping" last="Chen">Wanping Chen</name><affiliation><nlm:aff id="Aff16"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1790 4137</institution-id><institution-id institution-id-type="GRID">grid.35155.37</institution-id><institution>College of Food Science and Technology,</institution><institution>Huazhong Agricultural University,</institution></institution-wrap>Wuhan, 430070 China</nlm:aff></affiliation></author><author><name sortKey="Choi, Cindy" sort="Choi, Cindy" uniqKey="Choi C" first="Cindy" last="Choi">Cindy Choi</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Clum, Alicia" sort="Clum, Alicia" uniqKey="Clum A" first="Alicia" last="Clum">Alicia Clum</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Dos Santos, Renato Augusto Correa" sort="Dos Santos, Renato Augusto Correa" uniqKey="Dos Santos R" first="Renato Augusto Corrêa" last="Dos Santos">Renato Augusto Corrêa Dos Santos</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation></author><author><name sortKey="Damasio, Andre Ricardo De Lima" sort="Damasio, Andre Ricardo De Lima" uniqKey="Damasio A" first="André Ricardo De Lima" last="Damásio">André Ricardo De Lima Damásio</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation><affiliation><nlm:aff id="Aff17"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0723 2494</institution-id><institution-id institution-id-type="GRID">grid.411087.b</institution-id><institution>Department of Biochemistry and Tissue Biology,</institution><institution>Institute of Biology, University of Campinas,</institution></institution-wrap>CEP 13083-862 Campinas, SP Brazil</nlm:aff></affiliation></author><author><name sortKey="Diallinas, George" sort="Diallinas, George" uniqKey="Diallinas G" first="George" last="Diallinas">George Diallinas</name><affiliation><nlm:aff id="Aff5"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2155 0800</institution-id><institution-id institution-id-type="GRID">grid.5216.0</institution-id><institution>Department of Biology,</institution><institution>National and Kapodistrian University of Athens,</institution></institution-wrap>Panepistimioupolis, 15781 Athens, Greece</nlm:aff></affiliation></author><author><name sortKey="Emri, Tamas" sort="Emri, Tamas" uniqKey="Emri T" first="Tamás" last="Emri">Tamás Emri</name><affiliation><nlm:aff id="Aff18"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biotechnology and Microbiology, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>Egyetem tér 1, 4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Fekete, Erzsebet" sort="Fekete, Erzsebet" uniqKey="Fekete E" first="Erzsébet" last="Fekete">Erzsébet Fekete</name><affiliation><nlm:aff id="Aff8"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biochemical Engineering, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Flipphi, Michel" sort="Flipphi, Michel" uniqKey="Flipphi M" first="Michel" last="Flipphi">Michel Flipphi</name><affiliation><nlm:aff id="Aff8"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biochemical Engineering, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Freyberg, Susanne" sort="Freyberg, Susanne" uniqKey="Freyberg S" first="Susanne" last="Freyberg">Susanne Freyberg</name><affiliation><nlm:aff id="Aff10"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2364 4210</institution-id><institution-id institution-id-type="GRID">grid.7450.6</institution-id><institution>Department of Molecular Microbiology and Genetics,</institution><institution>Institute for Microbiology and Genetics, Georg August University Göttingen,</institution></institution-wrap>Grisebachstr. 8, 37077 Göttingen, Germany</nlm:aff></affiliation></author><author><name sortKey="Gallo, Antonia" sort="Gallo, Antonia" uniqKey="Gallo A" first="Antonia" last="Gallo">Antonia Gallo</name><affiliation><nlm:aff id="Aff19">Institute of Sciences of Food Production (ISPA), National Research Council (CNR), via Provinciale Lecce-Monteroni, 73100 Lecce, Italy</nlm:aff></affiliation></author><author><name sortKey="Gournas, Christos" sort="Gournas, Christos" uniqKey="Gournas C" first="Christos" last="Gournas">Christos Gournas</name><affiliation><nlm:aff id="Aff20">Institute of Biosciences and Applications, Microbial Molecular Genetics Laboratory, National Center for Scientific Research, Demokritos (NCSRD), Athens, Greece</nlm:aff></affiliation><affiliation><nlm:aff id="Aff62">Present address: Université Libre de Bruxelles Institute of Molecular Biology and Medicine (IBMM), Brussels, Belgium</nlm:aff></affiliation></author><author><name sortKey="Habgood, Rob" sort="Habgood, Rob" uniqKey="Habgood R" first="Rob" last="Habgood">Rob Habgood</name><affiliation><nlm:aff id="Aff21"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8868</institution-id><institution-id institution-id-type="GRID">grid.4563.4</institution-id><institution>School of Life Sciences,</institution><institution>University of Nottingham,</institution></institution-wrap>University Park, Nottingham, NG7 2RD UK</nlm:aff></affiliation></author><author><name sortKey="Hainaut, Matthieu" sort="Hainaut, Matthieu" uniqKey="Hainaut M" first="Matthieu" last="Hainaut">Matthieu Hainaut</name><affiliation><nlm:aff id="Aff22"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2176 4817</institution-id><institution-id institution-id-type="GRID">grid.5399.6</institution-id><institution></institution><institution>CNRS, Aix-Marseille Université,</institution></institution-wrap>Marseille, France</nlm:aff></affiliation></author><author><name sortKey="Harispe, Maria Laura" sort="Harispe, Maria Laura" uniqKey="Harispe M" first="María Laura" last="Harispe">María Laura Harispe</name><affiliation><nlm:aff id="Aff23"><institution-wrap><institution-id institution-id-type="GRID">grid.418532.9</institution-id><institution></institution><institution>Institut Pasteur de Montevideo, Unidad Mixta INIA-IPMont,</institution></institution-wrap>Mataojo 2020, CP11400 Montevideo, Uruguay</nlm:aff></affiliation><affiliation><nlm:aff id="Aff63">Present address: Instituto de Profesores Artigas, Consejo de Formación en Educación, ANEP, CP 11800, Av. del Libertador 2025, Montevideo, Uruguay</nlm:aff></affiliation></author><author><name sortKey="Henrissat, Bernard" sort="Henrissat, Bernard" uniqKey="Henrissat B" first="Bernard" last="Henrissat">Bernard Henrissat</name><affiliation><nlm:aff id="Aff22"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2176 4817</institution-id><institution-id institution-id-type="GRID">grid.5399.6</institution-id><institution></institution><institution>CNRS, Aix-Marseille Université,</institution></institution-wrap>Marseille, France</nlm:aff></affiliation><affiliation><nlm:aff id="Aff24">INRA, USC 1408 AFMB, 13288 Marseille, France</nlm:aff></affiliation><affiliation><nlm:aff id="Aff25"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0619 1117</institution-id><institution-id institution-id-type="GRID">grid.412125.1</institution-id><institution>Department of Biological Sciences,</institution><institution>King Abdulaziz University,</institution></institution-wrap>Jeddah, Saudi Arabia</nlm:aff></affiliation></author><author><name sortKey="Hilden, Kristiina S" sort="Hilden, Kristiina S" uniqKey="Hilden K" first="Kristiina S." last="Hildén">Kristiina S. Hildén</name><affiliation><nlm:aff id="Aff26"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0410 2071</institution-id><institution-id institution-id-type="GRID">grid.7737.4</institution-id><institution>Department of Food and Environmental Sciences,</institution><institution>University of Helsinki,</institution></institution-wrap>Viikinkaari 9, Helsinki, Finland</nlm:aff></affiliation></author><author><name sortKey="Hope, Ryan" sort="Hope, Ryan" uniqKey="Hope R" first="Ryan" last="Hope">Ryan Hope</name><affiliation><nlm:aff id="Aff21"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8868</institution-id><institution-id institution-id-type="GRID">grid.4563.4</institution-id><institution>School of Life Sciences,</institution><institution>University of Nottingham,</institution></institution-wrap>University Park, Nottingham, NG7 2RD UK</nlm:aff></affiliation></author><author><name sortKey="Hossain, Abeer" sort="Hossain, Abeer" uniqKey="Hossain A" first="Abeer" last="Hossain">Abeer Hossain</name><affiliation><nlm:aff id="Aff27">Dutch DNA Biotech BV, Utrechtseweg 48, 3703AJ Zeist, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff28"><institution-wrap><institution-id institution-id-type="ISNI">0000000084992262</institution-id><institution-id institution-id-type="GRID">grid.7177.6</institution-id><institution></institution><institution>Swammerdam Institute for Life Sciences, University of Amsterdam,</institution></institution-wrap>Amsterdam, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Karabika, Eugenia" sort="Karabika, Eugenia" uniqKey="Karabika E" first="Eugenia" last="Karabika">Eugenia Karabika</name><affiliation><nlm:aff id="Aff29"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0721 1626</institution-id><institution-id institution-id-type="GRID">grid.11914.3c</institution-id><institution>School of Biology,</institution><institution>University of St Andrews,</institution></institution-wrap>St Andrews, Fife KY16 9TH UK</nlm:aff></affiliation><affiliation><nlm:aff id="Aff64"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2108 7481</institution-id><institution-id institution-id-type="GRID">grid.9594.1</institution-id><institution>Present Address: Department of Chemistry,</institution><institution>University of Ioannina,</institution></institution-wrap>Ioannina, 45110 Greece</nlm:aff></affiliation></author><author><name sortKey="Karaffa, Levente" sort="Karaffa, Levente" uniqKey="Karaffa L" first="Levente" last="Karaffa">Levente Karaffa</name><affiliation><nlm:aff id="Aff8"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biochemical Engineering, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Karanyi, Zsolt" sort="Karanyi, Zsolt" uniqKey="Karanyi Z" first="Zsolt" last="Karányi">Zsolt Karányi</name><affiliation><nlm:aff id="Aff30"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Medicine, Faculty of Medicine,</institution><institution>University of Debrecen,</institution></institution-wrap>Nagyerdei krt. 98, 4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Krasevec, Nada" sort="Krasevec, Nada" uniqKey="Krasevec N" first="Nada" last="Kraševec">Nada Kraševec</name><affiliation><nlm:aff id="Aff7"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0661 0844</institution-id><institution-id institution-id-type="GRID">grid.454324.0</institution-id><institution>Laboratory for Molecular Biology and Nanobiotechnology,</institution><institution>National Institute of Chemistry,</institution></institution-wrap>Hajdrihova 19, 1000 Ljubljana, Slovenia</nlm:aff></affiliation></author><author><name sortKey="Kuo, Alan" sort="Kuo, Alan" uniqKey="Kuo A" first="Alan" last="Kuo">Alan Kuo</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Kusch, Harald" sort="Kusch, Harald" uniqKey="Kusch H" first="Harald" last="Kusch">Harald Kusch</name><affiliation><nlm:aff id="Aff10"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2364 4210</institution-id><institution-id institution-id-type="GRID">grid.7450.6</institution-id><institution>Department of Molecular Microbiology and Genetics,</institution><institution>Institute for Microbiology and Genetics, Georg August University Göttingen,</institution></institution-wrap>Grisebachstr. 8, 37077 Göttingen, Germany</nlm:aff></affiliation><affiliation><nlm:aff id="Aff31"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0482 5331</institution-id><institution-id institution-id-type="GRID">grid.411984.1</institution-id><institution>Department of Medical Informatics,</institution><institution>University Medical Centre,</institution></institution-wrap>Robert-Koch-Str.40, 37075 Göttingen, Germany</nlm:aff></affiliation><affiliation><nlm:aff id="Aff32"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0482 5331</institution-id><institution-id institution-id-type="GRID">grid.411984.1</institution-id><institution>Department of Molecular Biology,</institution><institution>Universitätsmedizin Göttingen,</institution></institution-wrap>Humboldtallee 23, Göttingen, 37073 Germany</nlm:aff></affiliation></author><author><name sortKey="Labutti, Kurt" sort="Labutti, Kurt" uniqKey="Labutti K" first="Kurt" last="Labutti">Kurt Labutti</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Lagendijk, Ellen L" sort="Lagendijk, Ellen L" uniqKey="Lagendijk E" first="Ellen L." last="Lagendijk">Ellen L. Lagendijk</name><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Lapidus, Alla" sort="Lapidus, Alla" uniqKey="Lapidus A" first="Alla" last="Lapidus">Alla Lapidus</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation><affiliation><nlm:aff id="Aff65"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2289 6897</institution-id><institution-id institution-id-type="GRID">grid.15447.33</institution-id><institution></institution><institution>Present address: Center for Algorithmic Biotechnology, St.Petersburg State University,</institution></institution-wrap>St. Petersburg, Russia</nlm:aff></affiliation></author><author><name sortKey="Levasseur, Anthony" sort="Levasseur, Anthony" uniqKey="Levasseur A" first="Anthony" last="Levasseur">Anthony Levasseur</name><affiliation><nlm:aff id="Aff33"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2176 4817</institution-id><institution-id institution-id-type="GRID">grid.5399.6</institution-id><institution></institution><institution>INRA, Aix-Marseille Univ, BBF, Biodiversité et Biotechnologie Fongiques,</institution></institution-wrap>Marseille, France</nlm:aff></affiliation><affiliation><nlm:aff id="Aff66"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0407 1584</institution-id><institution-id institution-id-type="GRID">grid.414336.7</institution-id><institution></institution><institution>Present address: Aix-Marseille Université, Unité de Recherche sur les Maladies Infectieuses et Tropicales Emergentes (URMITE), UM63, CNRS 7278, IRD 198, INSERM U1095, IHU Méditerranée Infection, Pôle des Maladies Infectieuses, Assistance Publique-Hôpitaux de Marseille, Faculté de Médecine,</institution></institution-wrap>27 Bd Jean Moulin, 13005 Marseille, France</nlm:aff></affiliation></author><author><name sortKey="Lindquist, Erika" sort="Lindquist, Erika" uniqKey="Lindquist E" first="Erika" last="Lindquist">Erika Lindquist</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Lipzen, Anna" sort="Lipzen, Anna" uniqKey="Lipzen A" first="Anna" last="Lipzen">Anna Lipzen</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Logrieco, Antonio F" sort="Logrieco, Antonio F" uniqKey="Logrieco A" first="Antonio F." last="Logrieco">Antonio F. Logrieco</name><affiliation><nlm:aff id="Aff34"><institution-wrap><institution-id institution-id-type="GRID">grid.473653.0</institution-id><institution></institution><institution>Institute of Sciences of Food Production (ISPA), National Research Council (CNR),</institution></institution-wrap>Via Amendola 122/O, 70126 Bari, Italy</nlm:aff></affiliation></author><author><name sortKey="Maccabe, Andrew" sort="Maccabe, Andrew" uniqKey="Maccabe A" first="Andrew" last="Maccabe">Andrew Maccabe</name><affiliation><nlm:aff id="Aff35"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1945 7738</institution-id><institution-id institution-id-type="GRID">grid.419051.8</institution-id><institution>Departamento de Biotecnología,</institution><institution>Instituto de Agroquímica y Tecnología de Alimentos, Consejo Superior de Investigaciones Científicas (CSIC),</institution></institution-wrap>Paterna, Valencia, Spain</nlm:aff></affiliation></author><author><name sortKey="M Kel, Miia R" sort="M Kel, Miia R" uniqKey="M Kel M" first="Miia R." last="M Kel">Miia R. M Kel</name><affiliation><nlm:aff id="Aff26"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0410 2071</institution-id><institution-id institution-id-type="GRID">grid.7737.4</institution-id><institution>Department of Food and Environmental Sciences,</institution><institution>University of Helsinki,</institution></institution-wrap>Viikinkaari 9, Helsinki, Finland</nlm:aff></affiliation></author><author><name sortKey="Malavazi, Iran" sort="Malavazi, Iran" uniqKey="Malavazi I" first="Iran" last="Malavazi">Iran Malavazi</name><affiliation><nlm:aff id="Aff36"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2163 588X</institution-id><institution-id institution-id-type="GRID">grid.411247.5</institution-id><institution>Departamento de Genética e Evolução,</institution><institution>Centro de Ciências Biológicas e da Saúde, Universidade Federal de São Carlos,</institution></institution-wrap>São Carlos, São Paulo Brazil</nlm:aff></affiliation></author><author><name sortKey="Melin, Petter" sort="Melin, Petter" uniqKey="Melin P" first="Petter" last="Melin">Petter Melin</name><affiliation><nlm:aff id="Aff37"><institution-wrap><institution-id institution-id-type="ISNI">0000 0000 8578 2742</institution-id><institution-id institution-id-type="GRID">grid.6341.0</institution-id><institution>Uppsala BioCenter, Department of Microbiology,</institution><institution>Swedish University of Agricultural Sciences,</institution></institution-wrap>P.O. Box 7025, 750 07 Uppsala, Sweden</nlm:aff></affiliation><affiliation><nlm:aff id="Aff67"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1523 2072</institution-id><institution-id institution-id-type="GRID">grid.437386.d</institution-id><institution></institution><institution>Present address: Swedish Chemicals Agency,</institution></institution-wrap>Box 2, 172 13 Sundbyberg, Sweden</nlm:aff></affiliation></author><author><name sortKey="Meyer, Vera" sort="Meyer, Vera" uniqKey="Meyer V" first="Vera" last="Meyer">Vera Meyer</name><affiliation><nlm:aff id="Aff38"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2292 8254</institution-id><institution-id institution-id-type="GRID">grid.6734.6</institution-id><institution>Institute of Biotechnology, Department Applied and Molecular Microbiology,</institution><institution>Berlin University of Technology,</institution></institution-wrap>Gustav-Meyer-Allee 25, 13355 Berlin, Germany</nlm:aff></affiliation></author><author><name sortKey="Mielnichuk, Natalia" sort="Mielnichuk, Natalia" uniqKey="Mielnichuk N" first="Natalia" last="Mielnichuk">Natalia Mielnichuk</name><affiliation><nlm:aff id="Aff13"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2168 1229</institution-id><institution-id institution-id-type="GRID">grid.9224.d</institution-id><institution>Department of Genetics, Faculty of Biology,</institution><institution>University of Seville,</institution></institution-wrap>Avda de Reina Mercedes 6, 41012 Sevilla, Spain</nlm:aff></affiliation><affiliation><nlm:aff id="Aff68">Present address: Instituto de Ciencia y Tecnología Dr. César Milstein, Fundación Pablo Cassará, CONICET, Saladillo 2468 C1440FFX, Ciudad de Buenos Aires, Argentina</nlm:aff></affiliation></author><author><name sortKey="Miskei, Marton" sort="Miskei, Marton" uniqKey="Miskei M" first="Márton" last="Miskei">Márton Miskei</name><affiliation><nlm:aff id="Aff18"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biotechnology and Microbiology, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>Egyetem tér 1, 4032 Debrecen, Hungary</nlm:aff></affiliation><affiliation><nlm:aff id="Aff39"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>MTA-DE Momentum, Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology,</institution><institution>University of Debrecen,</institution></institution-wrap>Nagyerdei krt.98., 4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Molnar, Akos P" sort="Molnar, Akos P" uniqKey="Molnar A" first="Ákos P." last="Molnár">Ákos P. Molnár</name><affiliation><nlm:aff id="Aff8"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biochemical Engineering, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Mule, Giuseppina" sort="Mule, Giuseppina" uniqKey="Mule G" first="Giuseppina" last="Mulé">Giuseppina Mulé</name><affiliation><nlm:aff id="Aff34"><institution-wrap><institution-id institution-id-type="GRID">grid.473653.0</institution-id><institution></institution><institution>Institute of Sciences of Food Production (ISPA), National Research Council (CNR),</institution></institution-wrap>Via Amendola 122/O, 70126 Bari, Italy</nlm:aff></affiliation></author><author><name sortKey="Ngan, Chew Yee" sort="Ngan, Chew Yee" uniqKey="Ngan C" first="Chew Yee" last="Ngan">Chew Yee Ngan</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Orejas, Margarita" sort="Orejas, Margarita" uniqKey="Orejas M" first="Margarita" last="Orejas">Margarita Orejas</name><affiliation><nlm:aff id="Aff35"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1945 7738</institution-id><institution-id institution-id-type="GRID">grid.419051.8</institution-id><institution>Departamento de Biotecnología,</institution><institution>Instituto de Agroquímica y Tecnología de Alimentos, Consejo Superior de Investigaciones Científicas (CSIC),</institution></institution-wrap>Paterna, Valencia, Spain</nlm:aff></affiliation></author><author><name sortKey="Orosz, Erzsebet" sort="Orosz, Erzsebet" uniqKey="Orosz E" first="Erzsébet" last="Orosz">Erzsébet Orosz</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff18"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biotechnology and Microbiology, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>Egyetem tér 1, 4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Ouedraogo, Jean Paul" sort="Ouedraogo, Jean Paul" uniqKey="Ouedraogo J" first="Jean Paul" last="Ouedraogo">Jean Paul Ouedraogo</name><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff69"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8630</institution-id><institution-id institution-id-type="GRID">grid.410319.e</institution-id><institution></institution><institution>Present address: Centre for Structural and Functional Genomics, Concordia University,</institution></institution-wrap>7141 Sherbrooke Street West, Montreal, QC H4B 1R6 Canada</nlm:aff></affiliation></author><author><name sortKey="Overkamp, Karin M" sort="Overkamp, Karin M" uniqKey="Overkamp K" first="Karin M." last="Overkamp">Karin M. Overkamp</name><affiliation><nlm:aff id="Aff27">Dutch DNA Biotech BV, Utrechtseweg 48, 3703AJ Zeist, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Park, Hee Soo" sort="Park, Hee Soo" uniqKey="Park H" first="Hee-Soo" last="Park">Hee-Soo Park</name><affiliation><nlm:aff id="Aff40"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0661 1556</institution-id><institution-id institution-id-type="GRID">grid.258803.4</institution-id><institution></institution><institution>School of Food Science and Biotechnology, Kyungpook National University,</institution></institution-wrap>Daegu, 702-701 Republic of Korea</nlm:aff></affiliation></author><author><name sortKey="Perrone, Giancarlo" sort="Perrone, Giancarlo" uniqKey="Perrone G" first="Giancarlo" last="Perrone">Giancarlo Perrone</name><affiliation><nlm:aff id="Aff34"><institution-wrap><institution-id institution-id-type="GRID">grid.473653.0</institution-id><institution></institution><institution>Institute of Sciences of Food Production (ISPA), National Research Council (CNR),</institution></institution-wrap>Via Amendola 122/O, 70126 Bari, Italy</nlm:aff></affiliation></author><author><name sortKey="Piumi, Francois" sort="Piumi, Francois" uniqKey="Piumi F" first="Francois" last="Piumi">Francois Piumi</name><affiliation><nlm:aff id="Aff33"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2176 4817</institution-id><institution-id institution-id-type="GRID">grid.5399.6</institution-id><institution></institution><institution>INRA, Aix-Marseille Univ, BBF, Biodiversité et Biotechnologie Fongiques,</institution></institution-wrap>Marseille, France</nlm:aff></affiliation><affiliation><nlm:aff id="Aff70">Present address: INRA UMR1198 Biologie du Développement et de la Reproduction - Domaine de Vilvert, Jouy en Josas, 78352 Cedex France</nlm:aff></affiliation></author><author><name sortKey="Punt, Peter J" sort="Punt, Peter J" uniqKey="Punt P" first="Peter J." last="Punt">Peter J. Punt</name><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff27">Dutch DNA Biotech BV, Utrechtseweg 48, 3703AJ Zeist, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Ram, Arthur F J" sort="Ram, Arthur F J" uniqKey="Ram A" first="Arthur F. J." last="Ram">Arthur F. J. Ram</name><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Ram N, Ana" sort="Ram N, Ana" uniqKey="Ram N A" first="Ana" last="Ram N">Ana Ram N</name><affiliation><nlm:aff id="Aff41"><institution-wrap><institution-id institution-id-type="ISNI">0000000121657640</institution-id><institution-id institution-id-type="GRID">grid.11630.35</institution-id><institution>Sección Bioquímica, Departamento de Biología Celular y Molecular, Facultad de Ciencias,</institution><institution>Universidad de la República,</institution></institution-wrap>Montevideo, Uruguay</nlm:aff></affiliation></author><author><name sortKey="Rauscher, Stefan" sort="Rauscher, Stefan" uniqKey="Rauscher S" first="Stefan" last="Rauscher">Stefan Rauscher</name><affiliation><nlm:aff id="Aff42"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0075 5874</institution-id><institution-id institution-id-type="GRID">grid.7892.4</institution-id><institution>Department of Microbiology,</institution><institution>Karlsruhe Institute of Technology, Institute for Applied Biosciences,</institution></institution-wrap>Hertzstrasse 16,, 76187 Karlsruhe, Germany</nlm:aff></affiliation></author><author><name sortKey="Record, Eric" sort="Record, Eric" uniqKey="Record E" first="Eric" last="Record">Eric Record</name><affiliation><nlm:aff id="Aff33"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2176 4817</institution-id><institution-id institution-id-type="GRID">grid.5399.6</institution-id><institution></institution><institution>INRA, Aix-Marseille Univ, BBF, Biodiversité et Biotechnologie Fongiques,</institution></institution-wrap>Marseille, France</nlm:aff></affiliation></author><author><name sortKey="Ria O Pach N, Diego Mauricio" sort="Ria O Pach N, Diego Mauricio" uniqKey="Ria O Pach N D" first="Diego Mauricio" last="Ria O-Pach N">Diego Mauricio Ria O-Pach N</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation></author><author><name sortKey="Robert, Vincent" sort="Robert, Vincent" uniqKey="Robert V" first="Vincent" last="Robert">Vincent Robert</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Rohrig, Julian" sort="Rohrig, Julian" uniqKey="Rohrig J" first="Julian" last="Röhrig">Julian Röhrig</name><affiliation><nlm:aff id="Aff42"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0075 5874</institution-id><institution-id institution-id-type="GRID">grid.7892.4</institution-id><institution>Department of Microbiology,</institution><institution>Karlsruhe Institute of Technology, Institute for Applied Biosciences,</institution></institution-wrap>Hertzstrasse 16,, 76187 Karlsruhe, Germany</nlm:aff></affiliation></author><author><name sortKey="Ruller, Roberto" sort="Ruller, Roberto" uniqKey="Ruller R" first="Roberto" last="Ruller">Roberto Ruller</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation></author><author><name sortKey="Salamov, Asaf" sort="Salamov, Asaf" uniqKey="Salamov A" first="Asaf" last="Salamov">Asaf Salamov</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Salih, Nadhira S" sort="Salih, Nadhira S" uniqKey="Salih N" first="Nadhira S." last="Salih">Nadhira S. Salih</name><affiliation><nlm:aff id="Aff21"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8868</institution-id><institution-id institution-id-type="GRID">grid.4563.4</institution-id><institution>School of Life Sciences,</institution><institution>University of Nottingham,</institution></institution-wrap>University Park, Nottingham, NG7 2RD UK</nlm:aff></affiliation><affiliation><nlm:aff id="Aff43">Department of Biology, School of Science, University of Sulaimani, Al Sulaymaneyah, Iraq</nlm:aff></affiliation></author><author><name sortKey="Samson, Rob A" sort="Samson, Rob A" uniqKey="Samson R" first="Rob A." last="Samson">Rob A. Samson</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Sandor, Erzsebet" sort="Sandor, Erzsebet" uniqKey="Sandor E" first="Erzsébet" last="Sándor">Erzsébet Sándor</name><affiliation><nlm:aff id="Aff44"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Institute of Food Science, Faculty of Agricultural and Food Sciences and Environmental Management,</institution><institution>University of Debrecen,</institution></institution-wrap>4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Sanguinetti, Manuel" sort="Sanguinetti, Manuel" uniqKey="Sanguinetti M" first="Manuel" last="Sanguinetti">Manuel Sanguinetti</name><affiliation><nlm:aff id="Aff41"><institution-wrap><institution-id institution-id-type="ISNI">0000000121657640</institution-id><institution-id institution-id-type="GRID">grid.11630.35</institution-id><institution>Sección Bioquímica, Departamento de Biología Celular y Molecular, Facultad de Ciencias,</institution><institution>Universidad de la República,</institution></institution-wrap>Montevideo, Uruguay</nlm:aff></affiliation></author><author><name sortKey="Schutze, Tabea" sort="Schutze, Tabea" uniqKey="Schutze T" first="Tabea" last="Schütze">Tabea Schütze</name><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff71"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2292 8254</institution-id><institution-id institution-id-type="GRID">grid.6734.6</institution-id><institution>Present address: Department Applied and Molecular Microbiology,</institution><institution>Institute of Biotechnology, Berlin University of Technology,</institution></institution-wrap>Gustav-Meyer-Allee 25, 13355 Berlin, Germany</nlm:aff></affiliation></author><author><name sortKey="Sep I, Kristina" sort="Sep I, Kristina" uniqKey="Sep I K" first="Kristina" last="Sep I">Kristina Sep I</name><affiliation><nlm:aff id="Aff45"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0721 6013</institution-id><institution-id institution-id-type="GRID">grid.8954.0</institution-id><institution>Department of Biology, Biotechnical Faculty,</institution><institution>University of Ljubljana,</institution></institution-wrap>Jamnikarjeva 101, 1000 Ljubljana, Slovenia</nlm:aff></affiliation></author><author><name sortKey="Shelest, Ekaterina" sort="Shelest, Ekaterina" uniqKey="Shelest E" first="Ekaterina" last="Shelest">Ekaterina Shelest</name><affiliation><nlm:aff id="Aff46"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0143 807X</institution-id><institution-id institution-id-type="GRID">grid.418398.f</institution-id><institution></institution><institution>Systems Biology/Bioinformatics group, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knoell Institute, (HKI),</institution></institution-wrap>Beutenbergstr. 11a, 07745 Jena, Germany</nlm:aff></affiliation></author><author><name sortKey="Sherlock, Gavin" sort="Sherlock, Gavin" uniqKey="Sherlock G" first="Gavin" last="Sherlock">Gavin Sherlock</name><affiliation><nlm:aff id="Aff47"><institution-wrap><institution-id institution-id-type="ISNI">0000000419368956</institution-id><institution-id institution-id-type="GRID">grid.168010.e</institution-id><institution>Department of Genetics,</institution><institution>Stanford University,</institution></institution-wrap>Stanford, CA 94305-5120 USA</nlm:aff></affiliation></author><author><name sortKey="Sophianopoulou, Vicky" sort="Sophianopoulou, Vicky" uniqKey="Sophianopoulou V" first="Vicky" last="Sophianopoulou">Vicky Sophianopoulou</name><affiliation><nlm:aff id="Aff20">Institute of Biosciences and Applications, Microbial Molecular Genetics Laboratory, National Center for Scientific Research, Demokritos (NCSRD), Athens, Greece</nlm:aff></affiliation></author><author><name sortKey="Squina, Fabio M" sort="Squina, Fabio M" uniqKey="Squina F" first="Fabio M." last="Squina">Fabio M. Squina</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation></author><author><name sortKey="Sun, Hui" sort="Sun, Hui" uniqKey="Sun H" first="Hui" last="Sun">Hui Sun</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Susca, Antonia" sort="Susca, Antonia" uniqKey="Susca A" first="Antonia" last="Susca">Antonia Susca</name><affiliation><nlm:aff id="Aff34"><institution-wrap><institution-id institution-id-type="GRID">grid.473653.0</institution-id><institution></institution><institution>Institute of Sciences of Food Production (ISPA), National Research Council (CNR),</institution></institution-wrap>Via Amendola 122/O, 70126 Bari, Italy</nlm:aff></affiliation></author><author><name sortKey="Todd, Richard B" sort="Todd, Richard B" uniqKey="Todd R" first="Richard B." last="Todd">Richard B. Todd</name><affiliation><nlm:aff id="Aff48"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0737 1259</institution-id><institution-id institution-id-type="GRID">grid.36567.31</institution-id><institution>Department of Plant Pathology,</institution><institution>Kansas State University,</institution></institution-wrap>Manhattan, KS 66506 USA</nlm:aff></affiliation></author><author><name sortKey="Tsang, Adrian" sort="Tsang, Adrian" uniqKey="Tsang A" first="Adrian" last="Tsang">Adrian Tsang</name><affiliation><nlm:aff id="Aff49"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8630</institution-id><institution-id institution-id-type="GRID">grid.410319.e</institution-id><institution></institution><institution>Centre for Structural and Functional Genomics, Concordia University,</institution></institution-wrap>7141 Sherbrooke Street West, Montreal, QC H4B 1R6 Canada</nlm:aff></affiliation></author><author><name sortKey="Unkles, Shiela E" sort="Unkles, Shiela E" uniqKey="Unkles S" first="Shiela E." last="Unkles">Shiela E. Unkles</name><affiliation><nlm:aff id="Aff29"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0721 1626</institution-id><institution-id institution-id-type="GRID">grid.11914.3c</institution-id><institution>School of Biology,</institution><institution>University of St Andrews,</institution></institution-wrap>St Andrews, Fife KY16 9TH UK</nlm:aff></affiliation></author><author><name sortKey="Van De Wiele, Nathalie" sort="Van De Wiele, Nathalie" uniqKey="Van De Wiele N" first="Nathalie" last="Van De Wiele">Nathalie Van De Wiele</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Van Rossen Uffink, Diana" sort="Van Rossen Uffink, Diana" uniqKey="Van Rossen Uffink D" first="Diana" last="Van Rossen-Uffink">Diana Van Rossen-Uffink</name><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff72">Present address: BaseClear B.V., Einsteinweg 5, 2333 CC Leiden, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Oliveira, Juliana Velasco De Castro" sort="Oliveira, Juliana Velasco De Castro" uniqKey="Oliveira J" first="Juliana Velasco De Castro" last="Oliveira">Juliana Velasco De Castro Oliveira</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation></author><author><name sortKey="Vesth, Tammi C" sort="Vesth, Tammi C" uniqKey="Vesth T" first="Tammi C." last="Vesth">Tammi C. Vesth</name><affiliation><nlm:aff id="Aff50"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2181 8870</institution-id><institution-id institution-id-type="GRID">grid.5170.3</institution-id><institution>Department of Biotechnology and Biomedicine,</institution><institution>Technical University of Denmark,</institution></institution-wrap>Søltofts Plads 223, 2800 Kongens Lyngby, Denmark</nlm:aff></affiliation></author><author><name sortKey="Visser, Jaap" sort="Visser, Jaap" uniqKey="Visser J" first="Jaap" last="Visser">Jaap Visser</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Yu, Jae Hyuk" sort="Yu, Jae Hyuk" uniqKey="Yu J" first="Jae-Hyuk" last="Yu">Jae-Hyuk Yu</name><affiliation><nlm:aff id="Aff51"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2167 3675</institution-id><institution-id institution-id-type="GRID">grid.14003.36</institution-id><institution>Departments of Bacteriology and Genetics,</institution><institution>University of Wisconsin-Madison,</institution></institution-wrap>1550 Linden Drive, Madison, WI 53706 USA</nlm:aff></affiliation></author><author><name sortKey="Zhou, Miaomiao" sort="Zhou, Miaomiao" uniqKey="Zhou M" first="Miaomiao" last="Zhou">Miaomiao Zhou</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000000120346234</institution-id><institution-id institution-id-type="GRID">grid.5477.1</institution-id><institution>Fungal Molecular Physiology,</institution><institution>Utrecht University,</institution></institution-wrap>Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Andersen, Mikael R" sort="Andersen, Mikael R" uniqKey="Andersen M" first="Mikael R." last="Andersen">Mikael R. Andersen</name><affiliation><nlm:aff id="Aff50"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2181 8870</institution-id><institution-id institution-id-type="GRID">grid.5170.3</institution-id><institution>Department of Biotechnology and Biomedicine,</institution><institution>Technical University of Denmark,</institution></institution-wrap>Søltofts Plads 223, 2800 Kongens Lyngby, Denmark</nlm:aff></affiliation></author><author><name sortKey="Archer, David B" sort="Archer, David B" uniqKey="Archer D" first="David B." last="Archer">David B. Archer</name><affiliation><nlm:aff id="Aff21"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8868</institution-id><institution-id institution-id-type="GRID">grid.4563.4</institution-id><institution>School of Life Sciences,</institution><institution>University of Nottingham,</institution></institution-wrap>University Park, Nottingham, NG7 2RD UK</nlm:aff></affiliation></author><author><name sortKey="Baker, Scott E" sort="Baker, Scott E" uniqKey="Baker S" first="Scott E." last="Baker">Scott E. Baker</name><affiliation><nlm:aff id="Aff52">Fungal Biotechnology Team, Pacific Northwest National Laboratory, Richland, Washington, 99352 USA</nlm:aff></affiliation></author><author><name sortKey="Benoit, Isabelle" sort="Benoit, Isabelle" uniqKey="Benoit I" first="Isabelle" last="Benoit">Isabelle Benoit</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000000120346234</institution-id><institution-id institution-id-type="GRID">grid.5477.1</institution-id><institution>Fungal Molecular Physiology,</institution><institution>Utrecht University,</institution></institution-wrap>Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff74"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8630</institution-id><institution-id institution-id-type="GRID">grid.410319.e</institution-id><institution></institution><institution>Present address: Centre of Functional and Structure Genomics Biology Department Concordia University,</institution></institution-wrap>7141 Sherbrooke St. W., Montreal, QC H4B 1R6 Canada</nlm:aff></affiliation></author><author><name sortKey="Brakhage, Axel A" sort="Brakhage, Axel A" uniqKey="Brakhage A" first="Axel A." last="Brakhage">Axel A. Brakhage</name><affiliation><nlm:aff id="Aff53"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1939 2794</institution-id><institution-id institution-id-type="GRID">grid.9613.d</institution-id><institution>Department of Molecular and Applied Microbiology,</institution><institution>Leibniz-Institute for Natural Product Research and Infection Biology - Hans Knoell Institute (HKI) and Institute for Microbiology, Friedrich Schiller University Jena,</institution></institution-wrap>Beutenbergstr. 11a, 07745 Jena, Germany</nlm:aff></affiliation></author><author><name sortKey="Braus, Gerhard H" sort="Braus, Gerhard H" uniqKey="Braus G" first="Gerhard H." last="Braus">Gerhard H. Braus</name><affiliation><nlm:aff id="Aff10"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2364 4210</institution-id><institution-id institution-id-type="GRID">grid.7450.6</institution-id><institution>Department of Molecular Microbiology and Genetics,</institution><institution>Institute for Microbiology and Genetics, Georg August University Göttingen,</institution></institution-wrap>Grisebachstr. 8, 37077 Göttingen, Germany</nlm:aff></affiliation></author><author><name sortKey="Fischer, Reinhard" sort="Fischer, Reinhard" uniqKey="Fischer R" first="Reinhard" last="Fischer">Reinhard Fischer</name><affiliation><nlm:aff id="Aff42"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0075 5874</institution-id><institution-id institution-id-type="GRID">grid.7892.4</institution-id><institution>Department of Microbiology,</institution><institution>Karlsruhe Institute of Technology, Institute for Applied Biosciences,</institution></institution-wrap>Hertzstrasse 16,, 76187 Karlsruhe, Germany</nlm:aff></affiliation></author><author><name sortKey="Frisvad, Jens C" sort="Frisvad, Jens C" uniqKey="Frisvad J" first="Jens C." last="Frisvad">Jens C. Frisvad</name><affiliation><nlm:aff id="Aff50"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2181 8870</institution-id><institution-id institution-id-type="GRID">grid.5170.3</institution-id><institution>Department of Biotechnology and Biomedicine,</institution><institution>Technical University of Denmark,</institution></institution-wrap>Søltofts Plads 223, 2800 Kongens Lyngby, Denmark</nlm:aff></affiliation></author><author><name sortKey="Goldman, Gustavo H" sort="Goldman, Gustavo H" uniqKey="Goldman G" first="Gustavo H." last="Goldman">Gustavo H. Goldman</name><affiliation><nlm:aff id="Aff54"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1937 0722</institution-id><institution-id institution-id-type="GRID">grid.11899.38</institution-id><institution>Faculdade de Ciências Farmacêuticas de Ribeirão Preto,</institution><institution>Universidade de São Paulo,</institution></institution-wrap>Av. do Café S/N, CEP 14040-903 Ribeirão Preto, São Paulo Brazil</nlm:aff></affiliation></author><author><name sortKey="Houbraken, Jos" sort="Houbraken, Jos" uniqKey="Houbraken J" first="Jos" last="Houbraken">Jos Houbraken</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Oakley, Berl" sort="Oakley, Berl" uniqKey="Oakley B" first="Berl" last="Oakley">Berl Oakley</name><affiliation><nlm:aff id="Aff55"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2106 0692</institution-id><institution-id institution-id-type="GRID">grid.266515.3</institution-id><institution>Department of Molecular Biosciences,</institution><institution>University of Kansas,</institution></institution-wrap>Lawrence, Kansas 66045 USA</nlm:aff></affiliation></author><author><name sortKey="P Csi, Istvan" sort="P Csi, Istvan" uniqKey="P Csi I" first="István" last="P Csi">István P Csi</name><affiliation><nlm:aff id="Aff18"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biotechnology and Microbiology, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>Egyetem tér 1, 4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Scazzocchio, Claudio" sort="Scazzocchio, Claudio" uniqKey="Scazzocchio C" first="Claudio" last="Scazzocchio">Claudio Scazzocchio</name><affiliation><nlm:aff id="Aff56"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2113 8111</institution-id><institution-id institution-id-type="GRID">grid.7445.2</institution-id><institution>Department of Microbiology,</institution><institution>Imperial College,</institution></institution-wrap>London, SW7 2AZ UK</nlm:aff></affiliation><affiliation><nlm:aff id="Aff57">Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris‐Sud, Université Paris‐Saclay, 91198 Gif‐sur‐Yvette cedex, France</nlm:aff></affiliation></author><author><name sortKey="Seiboth, Bernhard" sort="Seiboth, Bernhard" uniqKey="Seiboth B" first="Bernhard" last="Seiboth">Bernhard Seiboth</name><affiliation><nlm:aff id="Aff58"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2348 4034</institution-id><institution-id institution-id-type="GRID">grid.5329.d</institution-id><institution>Research Division Biochemical Technology,</institution><institution>Institute of Chemical Engineering, TU Wien,</institution></institution-wrap>Gumpendorferstraße 1a, 1060 Vienna, Austria</nlm:aff></affiliation></author><author><name sortKey="Vankuyk, Patricia A" sort="Vankuyk, Patricia A" uniqKey="Vankuyk P" first="Patricia A." last="Vankuyk">Patricia A. Vankuyk</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Wortman, Jennifer" sort="Wortman, Jennifer" uniqKey="Wortman J" first="Jennifer" last="Wortman">Jennifer Wortman</name><affiliation><nlm:aff id="Aff59"><institution-wrap><institution-id institution-id-type="GRID">grid.66859.34</institution-id><institution></institution><institution>Broad Institute,</institution></institution-wrap>415 Main St, Cambridge, MA 02142 USA</nlm:aff></affiliation><affiliation><nlm:aff id="Aff73">Present address: Seres Therapeutics, 200 Sidney St, Cambridge, MA 02139 USA</nlm:aff></affiliation></author><author><name sortKey="Dyer, Paul S" sort="Dyer, Paul S" uniqKey="Dyer P" first="Paul S." last="Dyer">Paul S. Dyer</name><affiliation><nlm:aff id="Aff21"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8868</institution-id><institution-id institution-id-type="GRID">grid.4563.4</institution-id><institution>School of Life Sciences,</institution><institution>University of Nottingham,</institution></institution-wrap>University Park, Nottingham, NG7 2RD UK</nlm:aff></affiliation></author><author><name sortKey="Grigoriev, Igor V" sort="Grigoriev, Igor V" uniqKey="Grigoriev I" first="Igor V." last="Grigoriev">Igor V. Grigoriev</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">28196534</idno><idno type="pmc">5307856</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5307856</idno><idno type="RBID">PMC:5307856</idno><idno type="doi">10.1186/s13059-017-1151-0</idno><date when="2017">2017</date><idno type="wicri:Area/Pmc/Corpus">000D10</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000D10</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Comparative genomics reveals high biological diversity and specific adaptations in the industrially and medically important fungal genus <italic>Aspergillus</italic></title><author><name sortKey="De Vries, Ronald P" sort="De Vries, Ronald P" uniqKey="De Vries R" first="Ronald P." last="De Vries">Ronald P. De Vries</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000000120346234</institution-id><institution-id institution-id-type="GRID">grid.5477.1</institution-id><institution>Fungal Molecular Physiology,</institution><institution>Utrecht University,</institution></institution-wrap>Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Riley, Robert" sort="Riley, Robert" uniqKey="Riley R" first="Robert" last="Riley">Robert Riley</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Wiebenga, Ad" sort="Wiebenga, Ad" uniqKey="Wiebenga A" first="Ad" last="Wiebenga">Ad Wiebenga</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000000120346234</institution-id><institution-id institution-id-type="GRID">grid.5477.1</institution-id><institution>Fungal Molecular Physiology,</institution><institution>Utrecht University,</institution></institution-wrap>Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Aguilar Osorio, Guillermo" sort="Aguilar Osorio, Guillermo" uniqKey="Aguilar Osorio G" first="Guillermo" last="Aguilar-Osorio">Guillermo Aguilar-Osorio</name><affiliation><nlm:aff id="Aff4"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2159 0001</institution-id><institution-id institution-id-type="GRID">grid.9486.3</institution-id><institution>Department of Food Science and Biotechnology, Faculty of Chemistry,</institution><institution>National University of Mexico,</institution></institution-wrap>Ciudad Universitaria, D.F. C.P. 04510 Mexico</nlm:aff></affiliation></author><author><name sortKey="Amillis, Sotiris" sort="Amillis, Sotiris" uniqKey="Amillis S" first="Sotiris" last="Amillis">Sotiris Amillis</name><affiliation><nlm:aff id="Aff5"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2155 0800</institution-id><institution-id institution-id-type="GRID">grid.5216.0</institution-id><institution>Department of Biology,</institution><institution>National and Kapodistrian University of Athens,</institution></institution-wrap>Panepistimioupolis, 15781 Athens, Greece</nlm:aff></affiliation></author><author><name sortKey="Uchima, Cristiane Akemi" sort="Uchima, Cristiane Akemi" uniqKey="Uchima C" first="Cristiane Akemi" last="Uchima">Cristiane Akemi Uchima</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation><affiliation><nlm:aff id="Aff60">Present address: VTT Brasil, Alameda Inajá, 123, CEP 06460-055 Barueri, São Paulo Brazil</nlm:aff></affiliation></author><author><name sortKey="Anderluh, Gregor" sort="Anderluh, Gregor" uniqKey="Anderluh G" first="Gregor" last="Anderluh">Gregor Anderluh</name><affiliation><nlm:aff id="Aff7"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0661 0844</institution-id><institution-id institution-id-type="GRID">grid.454324.0</institution-id><institution>Laboratory for Molecular Biology and Nanobiotechnology,</institution><institution>National Institute of Chemistry,</institution></institution-wrap>Hajdrihova 19, 1000 Ljubljana, Slovenia</nlm:aff></affiliation></author><author><name sortKey="Asadollahi, Mojtaba" sort="Asadollahi, Mojtaba" uniqKey="Asadollahi M" first="Mojtaba" last="Asadollahi">Mojtaba Asadollahi</name><affiliation><nlm:aff id="Aff8"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biochemical Engineering, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Askin, Marion" sort="Askin, Marion" uniqKey="Askin M" first="Marion" last="Askin">Marion Askin</name><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff61"><institution-wrap><institution-id institution-id-type="GRID">grid.431777.1</institution-id><institution></institution><institution>Present address: CSIRO Publishing,</institution></institution-wrap>Unipark, Building 1 Level 1, 195 Wellington Road, Clayton, VIC 3168 Australia</nlm:aff></affiliation></author><author><name sortKey="Barry, Kerrie" sort="Barry, Kerrie" uniqKey="Barry K" first="Kerrie" last="Barry">Kerrie Barry</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Battaglia, Evy" sort="Battaglia, Evy" uniqKey="Battaglia E" first="Evy" last="Battaglia">Evy Battaglia</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000000120346234</institution-id><institution-id institution-id-type="GRID">grid.5477.1</institution-id><institution>Fungal Molecular Physiology,</institution><institution>Utrecht University,</institution></institution-wrap>Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Bayram, Ozgur" sort="Bayram, Ozgur" uniqKey="Bayram O" first="Özgür" last="Bayram">Özgür Bayram</name><affiliation><nlm:aff id="Aff10"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2364 4210</institution-id><institution-id institution-id-type="GRID">grid.7450.6</institution-id><institution>Department of Molecular Microbiology and Genetics,</institution><institution>Institute for Microbiology and Genetics, Georg August University Göttingen,</institution></institution-wrap>Grisebachstr. 8, 37077 Göttingen, Germany</nlm:aff></affiliation><affiliation><nlm:aff id="Aff11"><institution-wrap><institution-id institution-id-type="ISNI">0000 0000 9331 9029</institution-id><institution-id institution-id-type="GRID">grid.95004.38</institution-id><institution>Department of Biology,</institution><institution>Maynooth University,</institution></institution-wrap>Maynooth, Co. Kildare Ireland</nlm:aff></affiliation></author><author><name sortKey="Benocci, Tiziano" sort="Benocci, Tiziano" uniqKey="Benocci T" first="Tiziano" last="Benocci">Tiziano Benocci</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000000120346234</institution-id><institution-id institution-id-type="GRID">grid.5477.1</institution-id><institution>Fungal Molecular Physiology,</institution><institution>Utrecht University,</institution></institution-wrap>Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Braus Stromeyer, Susanna A" sort="Braus Stromeyer, Susanna A" uniqKey="Braus Stromeyer S" first="Susanna A." last="Braus-Stromeyer">Susanna A. Braus-Stromeyer</name><affiliation><nlm:aff id="Aff10"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2364 4210</institution-id><institution-id institution-id-type="GRID">grid.7450.6</institution-id><institution>Department of Molecular Microbiology and Genetics,</institution><institution>Institute for Microbiology and Genetics, Georg August University Göttingen,</institution></institution-wrap>Grisebachstr. 8, 37077 Göttingen, Germany</nlm:aff></affiliation></author><author><name sortKey="Caldana, Camila" sort="Caldana, Camila" uniqKey="Caldana C" first="Camila" last="Caldana">Camila Caldana</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation><affiliation><nlm:aff id="Aff12">Max Planck Partner Group, Brazilian Bioethanol Science and Technology Laboratory, CEP 13083-100 Campinas, Sao Paulo Brazil</nlm:aff></affiliation></author><author><name sortKey="Canovas, David" sort="Canovas, David" uniqKey="Canovas D" first="David" last="Cánovas">David Cánovas</name><affiliation><nlm:aff id="Aff13"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2168 1229</institution-id><institution-id institution-id-type="GRID">grid.9224.d</institution-id><institution>Department of Genetics, Faculty of Biology,</institution><institution>University of Seville,</institution></institution-wrap>Avda de Reina Mercedes 6, 41012 Sevilla, Spain</nlm:aff></affiliation><affiliation><nlm:aff id="Aff14"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2298 5320</institution-id><institution-id institution-id-type="GRID">grid.5173.0</institution-id><institution>Fungal Genetics and Genomics Unit, Department of Applied Genetics and Cell Biology,</institution><institution>University of Natural Resources and Life Sciences (BOKU) Vienna,</institution></institution-wrap>Vienna, Austria</nlm:aff></affiliation></author><author><name sortKey="Cerqueira, Gustavo C" sort="Cerqueira, Gustavo C" uniqKey="Cerqueira G" first="Gustavo C." last="Cerqueira">Gustavo C. Cerqueira</name><affiliation><nlm:aff id="Aff15"><institution-wrap><institution-id institution-id-type="GRID">grid.66859.34</institution-id><institution></institution><institution>Broad Institute of Harvard and MIT,</institution></institution-wrap>75 Ames St, Cambridge, MA 02142 USA</nlm:aff></affiliation></author><author><name sortKey="Chen, Fusheng" sort="Chen, Fusheng" uniqKey="Chen F" first="Fusheng" last="Chen">Fusheng Chen</name><affiliation><nlm:aff id="Aff16"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1790 4137</institution-id><institution-id institution-id-type="GRID">grid.35155.37</institution-id><institution>College of Food Science and Technology,</institution><institution>Huazhong Agricultural University,</institution></institution-wrap>Wuhan, 430070 China</nlm:aff></affiliation></author><author><name sortKey="Chen, Wanping" sort="Chen, Wanping" uniqKey="Chen W" first="Wanping" last="Chen">Wanping Chen</name><affiliation><nlm:aff id="Aff16"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1790 4137</institution-id><institution-id institution-id-type="GRID">grid.35155.37</institution-id><institution>College of Food Science and Technology,</institution><institution>Huazhong Agricultural University,</institution></institution-wrap>Wuhan, 430070 China</nlm:aff></affiliation></author><author><name sortKey="Choi, Cindy" sort="Choi, Cindy" uniqKey="Choi C" first="Cindy" last="Choi">Cindy Choi</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Clum, Alicia" sort="Clum, Alicia" uniqKey="Clum A" first="Alicia" last="Clum">Alicia Clum</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Dos Santos, Renato Augusto Correa" sort="Dos Santos, Renato Augusto Correa" uniqKey="Dos Santos R" first="Renato Augusto Corrêa" last="Dos Santos">Renato Augusto Corrêa Dos Santos</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation></author><author><name sortKey="Damasio, Andre Ricardo De Lima" sort="Damasio, Andre Ricardo De Lima" uniqKey="Damasio A" first="André Ricardo De Lima" last="Damásio">André Ricardo De Lima Damásio</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation><affiliation><nlm:aff id="Aff17"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0723 2494</institution-id><institution-id institution-id-type="GRID">grid.411087.b</institution-id><institution>Department of Biochemistry and Tissue Biology,</institution><institution>Institute of Biology, University of Campinas,</institution></institution-wrap>CEP 13083-862 Campinas, SP Brazil</nlm:aff></affiliation></author><author><name sortKey="Diallinas, George" sort="Diallinas, George" uniqKey="Diallinas G" first="George" last="Diallinas">George Diallinas</name><affiliation><nlm:aff id="Aff5"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2155 0800</institution-id><institution-id institution-id-type="GRID">grid.5216.0</institution-id><institution>Department of Biology,</institution><institution>National and Kapodistrian University of Athens,</institution></institution-wrap>Panepistimioupolis, 15781 Athens, Greece</nlm:aff></affiliation></author><author><name sortKey="Emri, Tamas" sort="Emri, Tamas" uniqKey="Emri T" first="Tamás" last="Emri">Tamás Emri</name><affiliation><nlm:aff id="Aff18"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biotechnology and Microbiology, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>Egyetem tér 1, 4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Fekete, Erzsebet" sort="Fekete, Erzsebet" uniqKey="Fekete E" first="Erzsébet" last="Fekete">Erzsébet Fekete</name><affiliation><nlm:aff id="Aff8"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biochemical Engineering, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Flipphi, Michel" sort="Flipphi, Michel" uniqKey="Flipphi M" first="Michel" last="Flipphi">Michel Flipphi</name><affiliation><nlm:aff id="Aff8"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biochemical Engineering, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Freyberg, Susanne" sort="Freyberg, Susanne" uniqKey="Freyberg S" first="Susanne" last="Freyberg">Susanne Freyberg</name><affiliation><nlm:aff id="Aff10"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2364 4210</institution-id><institution-id institution-id-type="GRID">grid.7450.6</institution-id><institution>Department of Molecular Microbiology and Genetics,</institution><institution>Institute for Microbiology and Genetics, Georg August University Göttingen,</institution></institution-wrap>Grisebachstr. 8, 37077 Göttingen, Germany</nlm:aff></affiliation></author><author><name sortKey="Gallo, Antonia" sort="Gallo, Antonia" uniqKey="Gallo A" first="Antonia" last="Gallo">Antonia Gallo</name><affiliation><nlm:aff id="Aff19">Institute of Sciences of Food Production (ISPA), National Research Council (CNR), via Provinciale Lecce-Monteroni, 73100 Lecce, Italy</nlm:aff></affiliation></author><author><name sortKey="Gournas, Christos" sort="Gournas, Christos" uniqKey="Gournas C" first="Christos" last="Gournas">Christos Gournas</name><affiliation><nlm:aff id="Aff20">Institute of Biosciences and Applications, Microbial Molecular Genetics Laboratory, National Center for Scientific Research, Demokritos (NCSRD), Athens, Greece</nlm:aff></affiliation><affiliation><nlm:aff id="Aff62">Present address: Université Libre de Bruxelles Institute of Molecular Biology and Medicine (IBMM), Brussels, Belgium</nlm:aff></affiliation></author><author><name sortKey="Habgood, Rob" sort="Habgood, Rob" uniqKey="Habgood R" first="Rob" last="Habgood">Rob Habgood</name><affiliation><nlm:aff id="Aff21"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8868</institution-id><institution-id institution-id-type="GRID">grid.4563.4</institution-id><institution>School of Life Sciences,</institution><institution>University of Nottingham,</institution></institution-wrap>University Park, Nottingham, NG7 2RD UK</nlm:aff></affiliation></author><author><name sortKey="Hainaut, Matthieu" sort="Hainaut, Matthieu" uniqKey="Hainaut M" first="Matthieu" last="Hainaut">Matthieu Hainaut</name><affiliation><nlm:aff id="Aff22"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2176 4817</institution-id><institution-id institution-id-type="GRID">grid.5399.6</institution-id><institution></institution><institution>CNRS, Aix-Marseille Université,</institution></institution-wrap>Marseille, France</nlm:aff></affiliation></author><author><name sortKey="Harispe, Maria Laura" sort="Harispe, Maria Laura" uniqKey="Harispe M" first="María Laura" last="Harispe">María Laura Harispe</name><affiliation><nlm:aff id="Aff23"><institution-wrap><institution-id institution-id-type="GRID">grid.418532.9</institution-id><institution></institution><institution>Institut Pasteur de Montevideo, Unidad Mixta INIA-IPMont,</institution></institution-wrap>Mataojo 2020, CP11400 Montevideo, Uruguay</nlm:aff></affiliation><affiliation><nlm:aff id="Aff63">Present address: Instituto de Profesores Artigas, Consejo de Formación en Educación, ANEP, CP 11800, Av. del Libertador 2025, Montevideo, Uruguay</nlm:aff></affiliation></author><author><name sortKey="Henrissat, Bernard" sort="Henrissat, Bernard" uniqKey="Henrissat B" first="Bernard" last="Henrissat">Bernard Henrissat</name><affiliation><nlm:aff id="Aff22"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2176 4817</institution-id><institution-id institution-id-type="GRID">grid.5399.6</institution-id><institution></institution><institution>CNRS, Aix-Marseille Université,</institution></institution-wrap>Marseille, France</nlm:aff></affiliation><affiliation><nlm:aff id="Aff24">INRA, USC 1408 AFMB, 13288 Marseille, France</nlm:aff></affiliation><affiliation><nlm:aff id="Aff25"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0619 1117</institution-id><institution-id institution-id-type="GRID">grid.412125.1</institution-id><institution>Department of Biological Sciences,</institution><institution>King Abdulaziz University,</institution></institution-wrap>Jeddah, Saudi Arabia</nlm:aff></affiliation></author><author><name sortKey="Hilden, Kristiina S" sort="Hilden, Kristiina S" uniqKey="Hilden K" first="Kristiina S." last="Hildén">Kristiina S. Hildén</name><affiliation><nlm:aff id="Aff26"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0410 2071</institution-id><institution-id institution-id-type="GRID">grid.7737.4</institution-id><institution>Department of Food and Environmental Sciences,</institution><institution>University of Helsinki,</institution></institution-wrap>Viikinkaari 9, Helsinki, Finland</nlm:aff></affiliation></author><author><name sortKey="Hope, Ryan" sort="Hope, Ryan" uniqKey="Hope R" first="Ryan" last="Hope">Ryan Hope</name><affiliation><nlm:aff id="Aff21"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8868</institution-id><institution-id institution-id-type="GRID">grid.4563.4</institution-id><institution>School of Life Sciences,</institution><institution>University of Nottingham,</institution></institution-wrap>University Park, Nottingham, NG7 2RD UK</nlm:aff></affiliation></author><author><name sortKey="Hossain, Abeer" sort="Hossain, Abeer" uniqKey="Hossain A" first="Abeer" last="Hossain">Abeer Hossain</name><affiliation><nlm:aff id="Aff27">Dutch DNA Biotech BV, Utrechtseweg 48, 3703AJ Zeist, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff28"><institution-wrap><institution-id institution-id-type="ISNI">0000000084992262</institution-id><institution-id institution-id-type="GRID">grid.7177.6</institution-id><institution></institution><institution>Swammerdam Institute for Life Sciences, University of Amsterdam,</institution></institution-wrap>Amsterdam, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Karabika, Eugenia" sort="Karabika, Eugenia" uniqKey="Karabika E" first="Eugenia" last="Karabika">Eugenia Karabika</name><affiliation><nlm:aff id="Aff29"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0721 1626</institution-id><institution-id institution-id-type="GRID">grid.11914.3c</institution-id><institution>School of Biology,</institution><institution>University of St Andrews,</institution></institution-wrap>St Andrews, Fife KY16 9TH UK</nlm:aff></affiliation><affiliation><nlm:aff id="Aff64"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2108 7481</institution-id><institution-id institution-id-type="GRID">grid.9594.1</institution-id><institution>Present Address: Department of Chemistry,</institution><institution>University of Ioannina,</institution></institution-wrap>Ioannina, 45110 Greece</nlm:aff></affiliation></author><author><name sortKey="Karaffa, Levente" sort="Karaffa, Levente" uniqKey="Karaffa L" first="Levente" last="Karaffa">Levente Karaffa</name><affiliation><nlm:aff id="Aff8"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biochemical Engineering, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Karanyi, Zsolt" sort="Karanyi, Zsolt" uniqKey="Karanyi Z" first="Zsolt" last="Karányi">Zsolt Karányi</name><affiliation><nlm:aff id="Aff30"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Medicine, Faculty of Medicine,</institution><institution>University of Debrecen,</institution></institution-wrap>Nagyerdei krt. 98, 4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Krasevec, Nada" sort="Krasevec, Nada" uniqKey="Krasevec N" first="Nada" last="Kraševec">Nada Kraševec</name><affiliation><nlm:aff id="Aff7"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0661 0844</institution-id><institution-id institution-id-type="GRID">grid.454324.0</institution-id><institution>Laboratory for Molecular Biology and Nanobiotechnology,</institution><institution>National Institute of Chemistry,</institution></institution-wrap>Hajdrihova 19, 1000 Ljubljana, Slovenia</nlm:aff></affiliation></author><author><name sortKey="Kuo, Alan" sort="Kuo, Alan" uniqKey="Kuo A" first="Alan" last="Kuo">Alan Kuo</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Kusch, Harald" sort="Kusch, Harald" uniqKey="Kusch H" first="Harald" last="Kusch">Harald Kusch</name><affiliation><nlm:aff id="Aff10"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2364 4210</institution-id><institution-id institution-id-type="GRID">grid.7450.6</institution-id><institution>Department of Molecular Microbiology and Genetics,</institution><institution>Institute for Microbiology and Genetics, Georg August University Göttingen,</institution></institution-wrap>Grisebachstr. 8, 37077 Göttingen, Germany</nlm:aff></affiliation><affiliation><nlm:aff id="Aff31"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0482 5331</institution-id><institution-id institution-id-type="GRID">grid.411984.1</institution-id><institution>Department of Medical Informatics,</institution><institution>University Medical Centre,</institution></institution-wrap>Robert-Koch-Str.40, 37075 Göttingen, Germany</nlm:aff></affiliation><affiliation><nlm:aff id="Aff32"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0482 5331</institution-id><institution-id institution-id-type="GRID">grid.411984.1</institution-id><institution>Department of Molecular Biology,</institution><institution>Universitätsmedizin Göttingen,</institution></institution-wrap>Humboldtallee 23, Göttingen, 37073 Germany</nlm:aff></affiliation></author><author><name sortKey="Labutti, Kurt" sort="Labutti, Kurt" uniqKey="Labutti K" first="Kurt" last="Labutti">Kurt Labutti</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Lagendijk, Ellen L" sort="Lagendijk, Ellen L" uniqKey="Lagendijk E" first="Ellen L." last="Lagendijk">Ellen L. Lagendijk</name><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Lapidus, Alla" sort="Lapidus, Alla" uniqKey="Lapidus A" first="Alla" last="Lapidus">Alla Lapidus</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation><affiliation><nlm:aff id="Aff65"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2289 6897</institution-id><institution-id institution-id-type="GRID">grid.15447.33</institution-id><institution></institution><institution>Present address: Center for Algorithmic Biotechnology, St.Petersburg State University,</institution></institution-wrap>St. Petersburg, Russia</nlm:aff></affiliation></author><author><name sortKey="Levasseur, Anthony" sort="Levasseur, Anthony" uniqKey="Levasseur A" first="Anthony" last="Levasseur">Anthony Levasseur</name><affiliation><nlm:aff id="Aff33"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2176 4817</institution-id><institution-id institution-id-type="GRID">grid.5399.6</institution-id><institution></institution><institution>INRA, Aix-Marseille Univ, BBF, Biodiversité et Biotechnologie Fongiques,</institution></institution-wrap>Marseille, France</nlm:aff></affiliation><affiliation><nlm:aff id="Aff66"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0407 1584</institution-id><institution-id institution-id-type="GRID">grid.414336.7</institution-id><institution></institution><institution>Present address: Aix-Marseille Université, Unité de Recherche sur les Maladies Infectieuses et Tropicales Emergentes (URMITE), UM63, CNRS 7278, IRD 198, INSERM U1095, IHU Méditerranée Infection, Pôle des Maladies Infectieuses, Assistance Publique-Hôpitaux de Marseille, Faculté de Médecine,</institution></institution-wrap>27 Bd Jean Moulin, 13005 Marseille, France</nlm:aff></affiliation></author><author><name sortKey="Lindquist, Erika" sort="Lindquist, Erika" uniqKey="Lindquist E" first="Erika" last="Lindquist">Erika Lindquist</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Lipzen, Anna" sort="Lipzen, Anna" uniqKey="Lipzen A" first="Anna" last="Lipzen">Anna Lipzen</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Logrieco, Antonio F" sort="Logrieco, Antonio F" uniqKey="Logrieco A" first="Antonio F." last="Logrieco">Antonio F. Logrieco</name><affiliation><nlm:aff id="Aff34"><institution-wrap><institution-id institution-id-type="GRID">grid.473653.0</institution-id><institution></institution><institution>Institute of Sciences of Food Production (ISPA), National Research Council (CNR),</institution></institution-wrap>Via Amendola 122/O, 70126 Bari, Italy</nlm:aff></affiliation></author><author><name sortKey="Maccabe, Andrew" sort="Maccabe, Andrew" uniqKey="Maccabe A" first="Andrew" last="Maccabe">Andrew Maccabe</name><affiliation><nlm:aff id="Aff35"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1945 7738</institution-id><institution-id institution-id-type="GRID">grid.419051.8</institution-id><institution>Departamento de Biotecnología,</institution><institution>Instituto de Agroquímica y Tecnología de Alimentos, Consejo Superior de Investigaciones Científicas (CSIC),</institution></institution-wrap>Paterna, Valencia, Spain</nlm:aff></affiliation></author><author><name sortKey="M Kel, Miia R" sort="M Kel, Miia R" uniqKey="M Kel M" first="Miia R." last="M Kel">Miia R. M Kel</name><affiliation><nlm:aff id="Aff26"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0410 2071</institution-id><institution-id institution-id-type="GRID">grid.7737.4</institution-id><institution>Department of Food and Environmental Sciences,</institution><institution>University of Helsinki,</institution></institution-wrap>Viikinkaari 9, Helsinki, Finland</nlm:aff></affiliation></author><author><name sortKey="Malavazi, Iran" sort="Malavazi, Iran" uniqKey="Malavazi I" first="Iran" last="Malavazi">Iran Malavazi</name><affiliation><nlm:aff id="Aff36"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2163 588X</institution-id><institution-id institution-id-type="GRID">grid.411247.5</institution-id><institution>Departamento de Genética e Evolução,</institution><institution>Centro de Ciências Biológicas e da Saúde, Universidade Federal de São Carlos,</institution></institution-wrap>São Carlos, São Paulo Brazil</nlm:aff></affiliation></author><author><name sortKey="Melin, Petter" sort="Melin, Petter" uniqKey="Melin P" first="Petter" last="Melin">Petter Melin</name><affiliation><nlm:aff id="Aff37"><institution-wrap><institution-id institution-id-type="ISNI">0000 0000 8578 2742</institution-id><institution-id institution-id-type="GRID">grid.6341.0</institution-id><institution>Uppsala BioCenter, Department of Microbiology,</institution><institution>Swedish University of Agricultural Sciences,</institution></institution-wrap>P.O. Box 7025, 750 07 Uppsala, Sweden</nlm:aff></affiliation><affiliation><nlm:aff id="Aff67"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1523 2072</institution-id><institution-id institution-id-type="GRID">grid.437386.d</institution-id><institution></institution><institution>Present address: Swedish Chemicals Agency,</institution></institution-wrap>Box 2, 172 13 Sundbyberg, Sweden</nlm:aff></affiliation></author><author><name sortKey="Meyer, Vera" sort="Meyer, Vera" uniqKey="Meyer V" first="Vera" last="Meyer">Vera Meyer</name><affiliation><nlm:aff id="Aff38"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2292 8254</institution-id><institution-id institution-id-type="GRID">grid.6734.6</institution-id><institution>Institute of Biotechnology, Department Applied and Molecular Microbiology,</institution><institution>Berlin University of Technology,</institution></institution-wrap>Gustav-Meyer-Allee 25, 13355 Berlin, Germany</nlm:aff></affiliation></author><author><name sortKey="Mielnichuk, Natalia" sort="Mielnichuk, Natalia" uniqKey="Mielnichuk N" first="Natalia" last="Mielnichuk">Natalia Mielnichuk</name><affiliation><nlm:aff id="Aff13"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2168 1229</institution-id><institution-id institution-id-type="GRID">grid.9224.d</institution-id><institution>Department of Genetics, Faculty of Biology,</institution><institution>University of Seville,</institution></institution-wrap>Avda de Reina Mercedes 6, 41012 Sevilla, Spain</nlm:aff></affiliation><affiliation><nlm:aff id="Aff68">Present address: Instituto de Ciencia y Tecnología Dr. César Milstein, Fundación Pablo Cassará, CONICET, Saladillo 2468 C1440FFX, Ciudad de Buenos Aires, Argentina</nlm:aff></affiliation></author><author><name sortKey="Miskei, Marton" sort="Miskei, Marton" uniqKey="Miskei M" first="Márton" last="Miskei">Márton Miskei</name><affiliation><nlm:aff id="Aff18"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biotechnology and Microbiology, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>Egyetem tér 1, 4032 Debrecen, Hungary</nlm:aff></affiliation><affiliation><nlm:aff id="Aff39"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>MTA-DE Momentum, Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology,</institution><institution>University of Debrecen,</institution></institution-wrap>Nagyerdei krt.98., 4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Molnar, Akos P" sort="Molnar, Akos P" uniqKey="Molnar A" first="Ákos P." last="Molnár">Ákos P. Molnár</name><affiliation><nlm:aff id="Aff8"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biochemical Engineering, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Mule, Giuseppina" sort="Mule, Giuseppina" uniqKey="Mule G" first="Giuseppina" last="Mulé">Giuseppina Mulé</name><affiliation><nlm:aff id="Aff34"><institution-wrap><institution-id institution-id-type="GRID">grid.473653.0</institution-id><institution></institution><institution>Institute of Sciences of Food Production (ISPA), National Research Council (CNR),</institution></institution-wrap>Via Amendola 122/O, 70126 Bari, Italy</nlm:aff></affiliation></author><author><name sortKey="Ngan, Chew Yee" sort="Ngan, Chew Yee" uniqKey="Ngan C" first="Chew Yee" last="Ngan">Chew Yee Ngan</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Orejas, Margarita" sort="Orejas, Margarita" uniqKey="Orejas M" first="Margarita" last="Orejas">Margarita Orejas</name><affiliation><nlm:aff id="Aff35"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1945 7738</institution-id><institution-id institution-id-type="GRID">grid.419051.8</institution-id><institution>Departamento de Biotecnología,</institution><institution>Instituto de Agroquímica y Tecnología de Alimentos, Consejo Superior de Investigaciones Científicas (CSIC),</institution></institution-wrap>Paterna, Valencia, Spain</nlm:aff></affiliation></author><author><name sortKey="Orosz, Erzsebet" sort="Orosz, Erzsebet" uniqKey="Orosz E" first="Erzsébet" last="Orosz">Erzsébet Orosz</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff18"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biotechnology and Microbiology, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>Egyetem tér 1, 4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Ouedraogo, Jean Paul" sort="Ouedraogo, Jean Paul" uniqKey="Ouedraogo J" first="Jean Paul" last="Ouedraogo">Jean Paul Ouedraogo</name><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff69"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8630</institution-id><institution-id institution-id-type="GRID">grid.410319.e</institution-id><institution></institution><institution>Present address: Centre for Structural and Functional Genomics, Concordia University,</institution></institution-wrap>7141 Sherbrooke Street West, Montreal, QC H4B 1R6 Canada</nlm:aff></affiliation></author><author><name sortKey="Overkamp, Karin M" sort="Overkamp, Karin M" uniqKey="Overkamp K" first="Karin M." last="Overkamp">Karin M. Overkamp</name><affiliation><nlm:aff id="Aff27">Dutch DNA Biotech BV, Utrechtseweg 48, 3703AJ Zeist, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Park, Hee Soo" sort="Park, Hee Soo" uniqKey="Park H" first="Hee-Soo" last="Park">Hee-Soo Park</name><affiliation><nlm:aff id="Aff40"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0661 1556</institution-id><institution-id institution-id-type="GRID">grid.258803.4</institution-id><institution></institution><institution>School of Food Science and Biotechnology, Kyungpook National University,</institution></institution-wrap>Daegu, 702-701 Republic of Korea</nlm:aff></affiliation></author><author><name sortKey="Perrone, Giancarlo" sort="Perrone, Giancarlo" uniqKey="Perrone G" first="Giancarlo" last="Perrone">Giancarlo Perrone</name><affiliation><nlm:aff id="Aff34"><institution-wrap><institution-id institution-id-type="GRID">grid.473653.0</institution-id><institution></institution><institution>Institute of Sciences of Food Production (ISPA), National Research Council (CNR),</institution></institution-wrap>Via Amendola 122/O, 70126 Bari, Italy</nlm:aff></affiliation></author><author><name sortKey="Piumi, Francois" sort="Piumi, Francois" uniqKey="Piumi F" first="Francois" last="Piumi">Francois Piumi</name><affiliation><nlm:aff id="Aff33"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2176 4817</institution-id><institution-id institution-id-type="GRID">grid.5399.6</institution-id><institution></institution><institution>INRA, Aix-Marseille Univ, BBF, Biodiversité et Biotechnologie Fongiques,</institution></institution-wrap>Marseille, France</nlm:aff></affiliation><affiliation><nlm:aff id="Aff70">Present address: INRA UMR1198 Biologie du Développement et de la Reproduction - Domaine de Vilvert, Jouy en Josas, 78352 Cedex France</nlm:aff></affiliation></author><author><name sortKey="Punt, Peter J" sort="Punt, Peter J" uniqKey="Punt P" first="Peter J." last="Punt">Peter J. Punt</name><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff27">Dutch DNA Biotech BV, Utrechtseweg 48, 3703AJ Zeist, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Ram, Arthur F J" sort="Ram, Arthur F J" uniqKey="Ram A" first="Arthur F. J." last="Ram">Arthur F. J. Ram</name><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Ram N, Ana" sort="Ram N, Ana" uniqKey="Ram N A" first="Ana" last="Ram N">Ana Ram N</name><affiliation><nlm:aff id="Aff41"><institution-wrap><institution-id institution-id-type="ISNI">0000000121657640</institution-id><institution-id institution-id-type="GRID">grid.11630.35</institution-id><institution>Sección Bioquímica, Departamento de Biología Celular y Molecular, Facultad de Ciencias,</institution><institution>Universidad de la República,</institution></institution-wrap>Montevideo, Uruguay</nlm:aff></affiliation></author><author><name sortKey="Rauscher, Stefan" sort="Rauscher, Stefan" uniqKey="Rauscher S" first="Stefan" last="Rauscher">Stefan Rauscher</name><affiliation><nlm:aff id="Aff42"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0075 5874</institution-id><institution-id institution-id-type="GRID">grid.7892.4</institution-id><institution>Department of Microbiology,</institution><institution>Karlsruhe Institute of Technology, Institute for Applied Biosciences,</institution></institution-wrap>Hertzstrasse 16,, 76187 Karlsruhe, Germany</nlm:aff></affiliation></author><author><name sortKey="Record, Eric" sort="Record, Eric" uniqKey="Record E" first="Eric" last="Record">Eric Record</name><affiliation><nlm:aff id="Aff33"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2176 4817</institution-id><institution-id institution-id-type="GRID">grid.5399.6</institution-id><institution></institution><institution>INRA, Aix-Marseille Univ, BBF, Biodiversité et Biotechnologie Fongiques,</institution></institution-wrap>Marseille, France</nlm:aff></affiliation></author><author><name sortKey="Ria O Pach N, Diego Mauricio" sort="Ria O Pach N, Diego Mauricio" uniqKey="Ria O Pach N D" first="Diego Mauricio" last="Ria O-Pach N">Diego Mauricio Ria O-Pach N</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation></author><author><name sortKey="Robert, Vincent" sort="Robert, Vincent" uniqKey="Robert V" first="Vincent" last="Robert">Vincent Robert</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Rohrig, Julian" sort="Rohrig, Julian" uniqKey="Rohrig J" first="Julian" last="Röhrig">Julian Röhrig</name><affiliation><nlm:aff id="Aff42"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0075 5874</institution-id><institution-id institution-id-type="GRID">grid.7892.4</institution-id><institution>Department of Microbiology,</institution><institution>Karlsruhe Institute of Technology, Institute for Applied Biosciences,</institution></institution-wrap>Hertzstrasse 16,, 76187 Karlsruhe, Germany</nlm:aff></affiliation></author><author><name sortKey="Ruller, Roberto" sort="Ruller, Roberto" uniqKey="Ruller R" first="Roberto" last="Ruller">Roberto Ruller</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation></author><author><name sortKey="Salamov, Asaf" sort="Salamov, Asaf" uniqKey="Salamov A" first="Asaf" last="Salamov">Asaf Salamov</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Salih, Nadhira S" sort="Salih, Nadhira S" uniqKey="Salih N" first="Nadhira S." last="Salih">Nadhira S. Salih</name><affiliation><nlm:aff id="Aff21"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8868</institution-id><institution-id institution-id-type="GRID">grid.4563.4</institution-id><institution>School of Life Sciences,</institution><institution>University of Nottingham,</institution></institution-wrap>University Park, Nottingham, NG7 2RD UK</nlm:aff></affiliation><affiliation><nlm:aff id="Aff43">Department of Biology, School of Science, University of Sulaimani, Al Sulaymaneyah, Iraq</nlm:aff></affiliation></author><author><name sortKey="Samson, Rob A" sort="Samson, Rob A" uniqKey="Samson R" first="Rob A." last="Samson">Rob A. Samson</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Sandor, Erzsebet" sort="Sandor, Erzsebet" uniqKey="Sandor E" first="Erzsébet" last="Sándor">Erzsébet Sándor</name><affiliation><nlm:aff id="Aff44"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Institute of Food Science, Faculty of Agricultural and Food Sciences and Environmental Management,</institution><institution>University of Debrecen,</institution></institution-wrap>4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Sanguinetti, Manuel" sort="Sanguinetti, Manuel" uniqKey="Sanguinetti M" first="Manuel" last="Sanguinetti">Manuel Sanguinetti</name><affiliation><nlm:aff id="Aff41"><institution-wrap><institution-id institution-id-type="ISNI">0000000121657640</institution-id><institution-id institution-id-type="GRID">grid.11630.35</institution-id><institution>Sección Bioquímica, Departamento de Biología Celular y Molecular, Facultad de Ciencias,</institution><institution>Universidad de la República,</institution></institution-wrap>Montevideo, Uruguay</nlm:aff></affiliation></author><author><name sortKey="Schutze, Tabea" sort="Schutze, Tabea" uniqKey="Schutze T" first="Tabea" last="Schütze">Tabea Schütze</name><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff71"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2292 8254</institution-id><institution-id institution-id-type="GRID">grid.6734.6</institution-id><institution>Present address: Department Applied and Molecular Microbiology,</institution><institution>Institute of Biotechnology, Berlin University of Technology,</institution></institution-wrap>Gustav-Meyer-Allee 25, 13355 Berlin, Germany</nlm:aff></affiliation></author><author><name sortKey="Sep I, Kristina" sort="Sep I, Kristina" uniqKey="Sep I K" first="Kristina" last="Sep I">Kristina Sep I</name><affiliation><nlm:aff id="Aff45"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0721 6013</institution-id><institution-id institution-id-type="GRID">grid.8954.0</institution-id><institution>Department of Biology, Biotechnical Faculty,</institution><institution>University of Ljubljana,</institution></institution-wrap>Jamnikarjeva 101, 1000 Ljubljana, Slovenia</nlm:aff></affiliation></author><author><name sortKey="Shelest, Ekaterina" sort="Shelest, Ekaterina" uniqKey="Shelest E" first="Ekaterina" last="Shelest">Ekaterina Shelest</name><affiliation><nlm:aff id="Aff46"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0143 807X</institution-id><institution-id institution-id-type="GRID">grid.418398.f</institution-id><institution></institution><institution>Systems Biology/Bioinformatics group, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knoell Institute, (HKI),</institution></institution-wrap>Beutenbergstr. 11a, 07745 Jena, Germany</nlm:aff></affiliation></author><author><name sortKey="Sherlock, Gavin" sort="Sherlock, Gavin" uniqKey="Sherlock G" first="Gavin" last="Sherlock">Gavin Sherlock</name><affiliation><nlm:aff id="Aff47"><institution-wrap><institution-id institution-id-type="ISNI">0000000419368956</institution-id><institution-id institution-id-type="GRID">grid.168010.e</institution-id><institution>Department of Genetics,</institution><institution>Stanford University,</institution></institution-wrap>Stanford, CA 94305-5120 USA</nlm:aff></affiliation></author><author><name sortKey="Sophianopoulou, Vicky" sort="Sophianopoulou, Vicky" uniqKey="Sophianopoulou V" first="Vicky" last="Sophianopoulou">Vicky Sophianopoulou</name><affiliation><nlm:aff id="Aff20">Institute of Biosciences and Applications, Microbial Molecular Genetics Laboratory, National Center for Scientific Research, Demokritos (NCSRD), Athens, Greece</nlm:aff></affiliation></author><author><name sortKey="Squina, Fabio M" sort="Squina, Fabio M" uniqKey="Squina F" first="Fabio M." last="Squina">Fabio M. Squina</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation></author><author><name sortKey="Sun, Hui" sort="Sun, Hui" uniqKey="Sun H" first="Hui" last="Sun">Hui Sun</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author><author><name sortKey="Susca, Antonia" sort="Susca, Antonia" uniqKey="Susca A" first="Antonia" last="Susca">Antonia Susca</name><affiliation><nlm:aff id="Aff34"><institution-wrap><institution-id institution-id-type="GRID">grid.473653.0</institution-id><institution></institution><institution>Institute of Sciences of Food Production (ISPA), National Research Council (CNR),</institution></institution-wrap>Via Amendola 122/O, 70126 Bari, Italy</nlm:aff></affiliation></author><author><name sortKey="Todd, Richard B" sort="Todd, Richard B" uniqKey="Todd R" first="Richard B." last="Todd">Richard B. Todd</name><affiliation><nlm:aff id="Aff48"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0737 1259</institution-id><institution-id institution-id-type="GRID">grid.36567.31</institution-id><institution>Department of Plant Pathology,</institution><institution>Kansas State University,</institution></institution-wrap>Manhattan, KS 66506 USA</nlm:aff></affiliation></author><author><name sortKey="Tsang, Adrian" sort="Tsang, Adrian" uniqKey="Tsang A" first="Adrian" last="Tsang">Adrian Tsang</name><affiliation><nlm:aff id="Aff49"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8630</institution-id><institution-id institution-id-type="GRID">grid.410319.e</institution-id><institution></institution><institution>Centre for Structural and Functional Genomics, Concordia University,</institution></institution-wrap>7141 Sherbrooke Street West, Montreal, QC H4B 1R6 Canada</nlm:aff></affiliation></author><author><name sortKey="Unkles, Shiela E" sort="Unkles, Shiela E" uniqKey="Unkles S" first="Shiela E." last="Unkles">Shiela E. Unkles</name><affiliation><nlm:aff id="Aff29"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0721 1626</institution-id><institution-id institution-id-type="GRID">grid.11914.3c</institution-id><institution>School of Biology,</institution><institution>University of St Andrews,</institution></institution-wrap>St Andrews, Fife KY16 9TH UK</nlm:aff></affiliation></author><author><name sortKey="Van De Wiele, Nathalie" sort="Van De Wiele, Nathalie" uniqKey="Van De Wiele N" first="Nathalie" last="Van De Wiele">Nathalie Van De Wiele</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Van Rossen Uffink, Diana" sort="Van Rossen Uffink, Diana" uniqKey="Van Rossen Uffink D" first="Diana" last="Van Rossen-Uffink">Diana Van Rossen-Uffink</name><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff72">Present address: BaseClear B.V., Einsteinweg 5, 2333 CC Leiden, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Oliveira, Juliana Velasco De Castro" sort="Oliveira, Juliana Velasco De Castro" uniqKey="Oliveira J" first="Juliana Velasco De Castro" last="Oliveira">Juliana Velasco De Castro Oliveira</name><affiliation><nlm:aff id="Aff6"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</nlm:aff></affiliation></author><author><name sortKey="Vesth, Tammi C" sort="Vesth, Tammi C" uniqKey="Vesth T" first="Tammi C." last="Vesth">Tammi C. Vesth</name><affiliation><nlm:aff id="Aff50"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2181 8870</institution-id><institution-id institution-id-type="GRID">grid.5170.3</institution-id><institution>Department of Biotechnology and Biomedicine,</institution><institution>Technical University of Denmark,</institution></institution-wrap>Søltofts Plads 223, 2800 Kongens Lyngby, Denmark</nlm:aff></affiliation></author><author><name sortKey="Visser, Jaap" sort="Visser, Jaap" uniqKey="Visser J" first="Jaap" last="Visser">Jaap Visser</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Yu, Jae Hyuk" sort="Yu, Jae Hyuk" uniqKey="Yu J" first="Jae-Hyuk" last="Yu">Jae-Hyuk Yu</name><affiliation><nlm:aff id="Aff51"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2167 3675</institution-id><institution-id institution-id-type="GRID">grid.14003.36</institution-id><institution>Departments of Bacteriology and Genetics,</institution><institution>University of Wisconsin-Madison,</institution></institution-wrap>1550 Linden Drive, Madison, WI 53706 USA</nlm:aff></affiliation></author><author><name sortKey="Zhou, Miaomiao" sort="Zhou, Miaomiao" uniqKey="Zhou M" first="Miaomiao" last="Zhou">Miaomiao Zhou</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000000120346234</institution-id><institution-id institution-id-type="GRID">grid.5477.1</institution-id><institution>Fungal Molecular Physiology,</institution><institution>Utrecht University,</institution></institution-wrap>Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Andersen, Mikael R" sort="Andersen, Mikael R" uniqKey="Andersen M" first="Mikael R." last="Andersen">Mikael R. Andersen</name><affiliation><nlm:aff id="Aff50"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2181 8870</institution-id><institution-id institution-id-type="GRID">grid.5170.3</institution-id><institution>Department of Biotechnology and Biomedicine,</institution><institution>Technical University of Denmark,</institution></institution-wrap>Søltofts Plads 223, 2800 Kongens Lyngby, Denmark</nlm:aff></affiliation></author><author><name sortKey="Archer, David B" sort="Archer, David B" uniqKey="Archer D" first="David B." last="Archer">David B. Archer</name><affiliation><nlm:aff id="Aff21"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8868</institution-id><institution-id institution-id-type="GRID">grid.4563.4</institution-id><institution>School of Life Sciences,</institution><institution>University of Nottingham,</institution></institution-wrap>University Park, Nottingham, NG7 2RD UK</nlm:aff></affiliation></author><author><name sortKey="Baker, Scott E" sort="Baker, Scott E" uniqKey="Baker S" first="Scott E." last="Baker">Scott E. Baker</name><affiliation><nlm:aff id="Aff52">Fungal Biotechnology Team, Pacific Northwest National Laboratory, Richland, Washington, 99352 USA</nlm:aff></affiliation></author><author><name sortKey="Benoit, Isabelle" sort="Benoit, Isabelle" uniqKey="Benoit I" first="Isabelle" last="Benoit">Isabelle Benoit</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000000120346234</institution-id><institution-id institution-id-type="GRID">grid.5477.1</institution-id><institution>Fungal Molecular Physiology,</institution><institution>Utrecht University,</institution></institution-wrap>Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff74"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8630</institution-id><institution-id institution-id-type="GRID">grid.410319.e</institution-id><institution></institution><institution>Present address: Centre of Functional and Structure Genomics Biology Department Concordia University,</institution></institution-wrap>7141 Sherbrooke St. W., Montreal, QC H4B 1R6 Canada</nlm:aff></affiliation></author><author><name sortKey="Brakhage, Axel A" sort="Brakhage, Axel A" uniqKey="Brakhage A" first="Axel A." last="Brakhage">Axel A. Brakhage</name><affiliation><nlm:aff id="Aff53"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1939 2794</institution-id><institution-id institution-id-type="GRID">grid.9613.d</institution-id><institution>Department of Molecular and Applied Microbiology,</institution><institution>Leibniz-Institute for Natural Product Research and Infection Biology - Hans Knoell Institute (HKI) and Institute for Microbiology, Friedrich Schiller University Jena,</institution></institution-wrap>Beutenbergstr. 11a, 07745 Jena, Germany</nlm:aff></affiliation></author><author><name sortKey="Braus, Gerhard H" sort="Braus, Gerhard H" uniqKey="Braus G" first="Gerhard H." last="Braus">Gerhard H. Braus</name><affiliation><nlm:aff id="Aff10"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2364 4210</institution-id><institution-id institution-id-type="GRID">grid.7450.6</institution-id><institution>Department of Molecular Microbiology and Genetics,</institution><institution>Institute for Microbiology and Genetics, Georg August University Göttingen,</institution></institution-wrap>Grisebachstr. 8, 37077 Göttingen, Germany</nlm:aff></affiliation></author><author><name sortKey="Fischer, Reinhard" sort="Fischer, Reinhard" uniqKey="Fischer R" first="Reinhard" last="Fischer">Reinhard Fischer</name><affiliation><nlm:aff id="Aff42"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0075 5874</institution-id><institution-id institution-id-type="GRID">grid.7892.4</institution-id><institution>Department of Microbiology,</institution><institution>Karlsruhe Institute of Technology, Institute for Applied Biosciences,</institution></institution-wrap>Hertzstrasse 16,, 76187 Karlsruhe, Germany</nlm:aff></affiliation></author><author><name sortKey="Frisvad, Jens C" sort="Frisvad, Jens C" uniqKey="Frisvad J" first="Jens C." last="Frisvad">Jens C. Frisvad</name><affiliation><nlm:aff id="Aff50"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2181 8870</institution-id><institution-id institution-id-type="GRID">grid.5170.3</institution-id><institution>Department of Biotechnology and Biomedicine,</institution><institution>Technical University of Denmark,</institution></institution-wrap>Søltofts Plads 223, 2800 Kongens Lyngby, Denmark</nlm:aff></affiliation></author><author><name sortKey="Goldman, Gustavo H" sort="Goldman, Gustavo H" uniqKey="Goldman G" first="Gustavo H." last="Goldman">Gustavo H. Goldman</name><affiliation><nlm:aff id="Aff54"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1937 0722</institution-id><institution-id institution-id-type="GRID">grid.11899.38</institution-id><institution>Faculdade de Ciências Farmacêuticas de Ribeirão Preto,</institution><institution>Universidade de São Paulo,</institution></institution-wrap>Av. do Café S/N, CEP 14040-903 Ribeirão Preto, São Paulo Brazil</nlm:aff></affiliation></author><author><name sortKey="Houbraken, Jos" sort="Houbraken, Jos" uniqKey="Houbraken J" first="Jos" last="Houbraken">Jos Houbraken</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Oakley, Berl" sort="Oakley, Berl" uniqKey="Oakley B" first="Berl" last="Oakley">Berl Oakley</name><affiliation><nlm:aff id="Aff55"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2106 0692</institution-id><institution-id institution-id-type="GRID">grid.266515.3</institution-id><institution>Department of Molecular Biosciences,</institution><institution>University of Kansas,</institution></institution-wrap>Lawrence, Kansas 66045 USA</nlm:aff></affiliation></author><author><name sortKey="P Csi, Istvan" sort="P Csi, Istvan" uniqKey="P Csi I" first="István" last="P Csi">István P Csi</name><affiliation><nlm:aff id="Aff18"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biotechnology and Microbiology, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>Egyetem tér 1, 4032 Debrecen, Hungary</nlm:aff></affiliation></author><author><name sortKey="Scazzocchio, Claudio" sort="Scazzocchio, Claudio" uniqKey="Scazzocchio C" first="Claudio" last="Scazzocchio">Claudio Scazzocchio</name><affiliation><nlm:aff id="Aff56"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2113 8111</institution-id><institution-id institution-id-type="GRID">grid.7445.2</institution-id><institution>Department of Microbiology,</institution><institution>Imperial College,</institution></institution-wrap>London, SW7 2AZ UK</nlm:aff></affiliation><affiliation><nlm:aff id="Aff57">Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris‐Sud, Université Paris‐Saclay, 91198 Gif‐sur‐Yvette cedex, France</nlm:aff></affiliation></author><author><name sortKey="Seiboth, Bernhard" sort="Seiboth, Bernhard" uniqKey="Seiboth B" first="Bernhard" last="Seiboth">Bernhard Seiboth</name><affiliation><nlm:aff id="Aff58"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2348 4034</institution-id><institution-id institution-id-type="GRID">grid.5329.d</institution-id><institution>Research Division Biochemical Technology,</institution><institution>Institute of Chemical Engineering, TU Wien,</institution></institution-wrap>Gumpendorferstraße 1a, 1060 Vienna, Austria</nlm:aff></affiliation></author><author><name sortKey="Vankuyk, Patricia A" sort="Vankuyk, Patricia A" uniqKey="Vankuyk P" first="Patricia A." last="Vankuyk">Patricia A. Vankuyk</name><affiliation><nlm:aff id="Aff1">Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</nlm:aff></affiliation><affiliation><nlm:aff id="Aff9"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</nlm:aff></affiliation></author><author><name sortKey="Wortman, Jennifer" sort="Wortman, Jennifer" uniqKey="Wortman J" first="Jennifer" last="Wortman">Jennifer Wortman</name><affiliation><nlm:aff id="Aff59"><institution-wrap><institution-id institution-id-type="GRID">grid.66859.34</institution-id><institution></institution><institution>Broad Institute,</institution></institution-wrap>415 Main St, Cambridge, MA 02142 USA</nlm:aff></affiliation><affiliation><nlm:aff id="Aff73">Present address: Seres Therapeutics, 200 Sidney St, Cambridge, MA 02139 USA</nlm:aff></affiliation></author><author><name sortKey="Dyer, Paul S" sort="Dyer, Paul S" uniqKey="Dyer P" first="Paul S." last="Dyer">Paul S. Dyer</name><affiliation><nlm:aff id="Aff21"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8868</institution-id><institution-id institution-id-type="GRID">grid.4563.4</institution-id><institution>School of Life Sciences,</institution><institution>University of Nottingham,</institution></institution-wrap>University Park, Nottingham, NG7 2RD UK</nlm:aff></affiliation></author><author><name sortKey="Grigoriev, Igor V" sort="Grigoriev, Igor V" uniqKey="Grigoriev I" first="Igor V." last="Grigoriev">Igor V. Grigoriev</name><affiliation><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</nlm:aff></affiliation></author></analytic><series><title level="j">Genome Biology</title><idno type="ISSN">1474-7596</idno><idno type="eISSN">1474-760X</idno><imprint><date when="2017">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><sec><title>Background</title><p>The fungal genus <italic>Aspergillus</italic> is of critical importance to humankind. Species include those with industrial applications, important pathogens of humans, animals and crops, a source of potent carcinogenic contaminants of food, and an important genetic model. The genome sequences of eight aspergilli have already been explored to investigate aspects of fungal biology, raising questions about evolution and specialization within this genus.</p></sec><sec><title>Results</title><p>We have generated genome sequences for ten novel, highly diverse <italic>Aspergillus</italic> species and compared these in detail to sister and more distant genera. Comparative studies of key aspects of fungal biology, including primary and secondary metabolism, stress response, biomass degradation, and signal transduction, revealed both conservation and diversity among the species. Observed genomic differences were validated with experimental studies. This revealed several highlights, such as the potential for sex in asexual species, organic acid production genes being a key feature of black aspergilli, alternative approaches for degrading plant biomass, and indications for the genetic basis of stress response. A genome-wide phylogenetic analysis demonstrated in detail the relationship of the newly genome sequenced species with other aspergilli.</p></sec><sec><title>Conclusions</title><p>Many aspects of biological differences between fungal species cannot be explained by current knowledge obtained from genome sequences. The comparative genomics and experimental study, presented here, allows for the first time a genus-wide view of the biological diversity of the aspergilli and in many, but not all, cases linked genome differences to phenotype. Insights gained could be exploited for biotechnological and medical applications of fungi.</p></sec><sec><title>Electronic supplementary material</title><p>The online version of this article (doi:10.1186/s13059-017-1151-0) contains supplementary material, which is available to authorized users.</p></sec></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Samson, Ra" uniqKey="Samson R">RA Samson</name></author><author><name sortKey="Visagie, Cm" uniqKey="Visagie C">CM Visagie</name></author><author><name sortKey="Houbraken, J" uniqKey="Houbraken J">J Houbraken</name></author><author><name sortKey="Hong, Sb" uniqKey="Hong S">SB Hong</name></author><author><name sortKey="Hubka, V" uniqKey="Hubka V">V Hubka</name></author><author><name sortKey="Klaassen, Ch" uniqKey="Klaassen C">CH Klaassen</name></author></analytic></biblStruct><biblStruct></biblStruct><biblStruct><analytic><author><name sortKey="Geiser, Dm" uniqKey="Geiser D">DM Geiser</name></author><author><name sortKey="Samson, Ra" uniqKey="Samson R">RA Samson</name></author><author><name sortKey="Varga, J" uniqKey="Varga J">J Varga</name></author><author><name sortKey="Rokas, A" uniqKey="Rokas A">A Rokas</name></author><author><name sortKey="Witiak, Sm" uniqKey="Witiak S">SM Witiak</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Galagan, Je" uniqKey="Galagan J">JE Galagan</name></author><author><name sortKey="Calvo, Se" uniqKey="Calvo S">SE Calvo</name></author><author><name sortKey="Cuomo, C" uniqKey="Cuomo C">C Cuomo</name></author><author><name sortKey="Ma, Lj" uniqKey="Ma L">LJ Ma</name></author><author><name sortKey="Wortman, Jr" uniqKey="Wortman J">JR Wortman</name></author><author><name sortKey="Batzoglou, S" uniqKey="Batzoglou S">S Batzoglou</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Machida, M" uniqKey="Machida M">M Machida</name></author><author><name sortKey="Asai, K" uniqKey="Asai K">K Asai</name></author><author><name sortKey="Sano, M" uniqKey="Sano M">M Sano</name></author><author><name sortKey="Tanaka, T" uniqKey="Tanaka T">T Tanaka</name></author><author><name sortKey="Kumagai, T" uniqKey="Kumagai T">T Kumagai</name></author><author><name sortKey="Terai, G" uniqKey="Terai G">G Terai</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Nierman, Wc" uniqKey="Nierman W">WC Nierman</name></author><author><name sortKey="Pain, A" uniqKey="Pain A">A Pain</name></author><author><name sortKey="Anderson, Mj" uniqKey="Anderson M">MJ Anderson</name></author><author><name sortKey="Wortman, Jr" uniqKey="Wortman J">JR Wortman</name></author><author><name sortKey="Kim, Hs" uniqKey="Kim H">HS Kim</name></author><author><name sortKey="Arroyo, J" uniqKey="Arroyo J">J Arroyo</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Andersen, Mr" uniqKey="Andersen M">MR Andersen</name></author><author><name sortKey="Salazar, Mp" uniqKey="Salazar M">MP Salazar</name></author><author><name sortKey="Schaap, Pj" uniqKey="Schaap P">PJ Schaap</name></author><author><name sortKey="Van De Vondervoort, Pj" uniqKey="Van De Vondervoort P">PJ van de Vondervoort</name></author><author><name sortKey="Culley, D" uniqKey="Culley D">D Culley</name></author><author><name sortKey="Thykaer, J" uniqKey="Thykaer J">J Thykaer</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Fedorova, Nd" uniqKey="Fedorova N">ND Fedorova</name></author><author><name sortKey="Khaldi, N" uniqKey="Khaldi N">N Khaldi</name></author><author><name sortKey="Joardar, Vs" uniqKey="Joardar V">VS Joardar</name></author><author><name sortKey="Maiti, R" uniqKey="Maiti R">R Maiti</name></author><author><name sortKey="Amedeo, P" uniqKey="Amedeo P">P Amedeo</name></author><author><name sortKey="Anderson, Mj" uniqKey="Anderson M">MJ 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Genome Biol</journal-id><journal-id journal-id-type="iso-abbrev">Genome Biol</journal-id><journal-title-group><journal-title>Genome Biology</journal-title></journal-title-group><issn pub-type="ppub">1474-7596</issn><issn pub-type="epub">1474-760X</issn><publisher><publisher-name>BioMed Central</publisher-name><publisher-loc>London</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">28196534</article-id><article-id pub-id-type="pmc">5307856</article-id><article-id pub-id-type="publisher-id">1151</article-id><article-id pub-id-type="doi">10.1186/s13059-017-1151-0</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research</subject></subj-group></article-categories><title-group><article-title>Comparative genomics reveals high biological diversity and specific adaptations in the industrially and medically important fungal genus 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contrib-type="author"><name><surname>Grigoriev</surname><given-names>Igor V.</given-names></name><address><email>ivgrigoriev@lbl.gov</email></address><xref ref-type="aff" rid="Aff3">3</xref></contrib><aff id="Aff1"><label>1</label>Westerdijk Fungal Biodiversity Institute, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</aff><aff id="Aff2"><label>2</label><institution-wrap><institution-id institution-id-type="ISNI">0000000120346234</institution-id><institution-id institution-id-type="GRID">grid.5477.1</institution-id><institution>Fungal Molecular Physiology,</institution><institution>Utrecht University,</institution></institution-wrap>Uppsalalaan 8, 3584 CT Utrecht, The Netherlands</aff><aff id="Aff3"><label>3</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0449 479X</institution-id><institution-id institution-id-type="GRID">grid.451309.a</institution-id><institution></institution><institution>US Department of Energy Joint Genome Institute,</institution></institution-wrap>2800 Mitchell Drive, Walnut Creek, CA 94598 USA</aff><aff id="Aff4"><label>4</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2159 0001</institution-id><institution-id institution-id-type="GRID">grid.9486.3</institution-id><institution>Department of Food Science and Biotechnology, Faculty of Chemistry,</institution><institution>National University of Mexico,</institution></institution-wrap>Ciudad Universitaria, D.F. C.P. 04510 Mexico</aff><aff id="Aff5"><label>5</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2155 0800</institution-id><institution-id institution-id-type="GRID">grid.5216.0</institution-id><institution>Department of Biology,</institution><institution>National and Kapodistrian University of Athens,</institution></institution-wrap>Panepistimioupolis, 15781 Athens, Greece</aff><aff id="Aff6"><label>6</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0445 0877</institution-id><institution-id institution-id-type="GRID">grid.452567.7</institution-id><institution>Laboratório Nacional de Ciência e Tecnologia do Bioetanol (CTBE),</institution><institution>Centro Nacional de Pesquisa em Energia e Materiais (CNPEM),</institution></institution-wrap>Caixa Postal 6192 CEP 13083-970, Campinas, São Paulo Brasil</aff><aff id="Aff7"><label>7</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0661 0844</institution-id><institution-id institution-id-type="GRID">grid.454324.0</institution-id><institution>Laboratory for Molecular Biology and Nanobiotechnology,</institution><institution>National Institute of Chemistry,</institution></institution-wrap>Hajdrihova 19, 1000 Ljubljana, Slovenia</aff><aff id="Aff8"><label>8</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biochemical Engineering, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>4032 Debrecen, Hungary</aff><aff id="Aff9"><label>9</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2312 1970</institution-id><institution-id institution-id-type="GRID">grid.5132.5</institution-id><institution></institution><institution>Institute of Biology Leiden, Molecular Microbiology and Biotechnology, Leiden University,</institution></institution-wrap>Sylviusweg 72, 2333 BE Leiden, The Netherlands</aff><aff id="Aff10"><label>10</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2364 4210</institution-id><institution-id institution-id-type="GRID">grid.7450.6</institution-id><institution>Department of Molecular Microbiology and Genetics,</institution><institution>Institute for Microbiology and Genetics, Georg August University Göttingen,</institution></institution-wrap>Grisebachstr. 8, 37077 Göttingen, Germany</aff><aff id="Aff11"><label>11</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0000 9331 9029</institution-id><institution-id institution-id-type="GRID">grid.95004.38</institution-id><institution>Department of Biology,</institution><institution>Maynooth University,</institution></institution-wrap>Maynooth, Co. Kildare Ireland</aff><aff id="Aff12"><label>12</label>Max Planck Partner Group, Brazilian Bioethanol Science and Technology Laboratory, CEP 13083-100 Campinas, Sao Paulo Brazil</aff><aff id="Aff13"><label>13</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2168 1229</institution-id><institution-id institution-id-type="GRID">grid.9224.d</institution-id><institution>Department of Genetics, Faculty of Biology,</institution><institution>University of Seville,</institution></institution-wrap>Avda de Reina Mercedes 6, 41012 Sevilla, Spain</aff><aff id="Aff14"><label>14</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2298 5320</institution-id><institution-id institution-id-type="GRID">grid.5173.0</institution-id><institution>Fungal Genetics and Genomics Unit, Department of Applied Genetics and Cell Biology,</institution><institution>University of Natural Resources and Life Sciences (BOKU) Vienna,</institution></institution-wrap>Vienna, Austria</aff><aff id="Aff15"><label>15</label><institution-wrap><institution-id institution-id-type="GRID">grid.66859.34</institution-id><institution></institution><institution>Broad Institute of Harvard and MIT,</institution></institution-wrap>75 Ames St, Cambridge, MA 02142 USA</aff><aff id="Aff16"><label>16</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1790 4137</institution-id><institution-id institution-id-type="GRID">grid.35155.37</institution-id><institution>College of Food Science and Technology,</institution><institution>Huazhong Agricultural University,</institution></institution-wrap>Wuhan, 430070 China</aff><aff id="Aff17"><label>17</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0723 2494</institution-id><institution-id institution-id-type="GRID">grid.411087.b</institution-id><institution>Department of Biochemistry and Tissue Biology,</institution><institution>Institute of Biology, University of Campinas,</institution></institution-wrap>CEP 13083-862 Campinas, SP Brazil</aff><aff id="Aff18"><label>18</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Biotechnology and Microbiology, Faculty of Science and Technology,</institution><institution>University of Debrecen,</institution></institution-wrap>Egyetem tér 1, 4032 Debrecen, Hungary</aff><aff id="Aff19"><label>19</label>Institute of Sciences of Food Production (ISPA), National Research Council (CNR), via Provinciale Lecce-Monteroni, 73100 Lecce, Italy</aff><aff id="Aff20"><label>20</label>Institute of Biosciences and Applications, Microbial Molecular Genetics Laboratory, National Center for Scientific Research, Demokritos (NCSRD), Athens, Greece</aff><aff id="Aff21"><label>21</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8868</institution-id><institution-id institution-id-type="GRID">grid.4563.4</institution-id><institution>School of Life Sciences,</institution><institution>University of Nottingham,</institution></institution-wrap>University Park, Nottingham, NG7 2RD UK</aff><aff id="Aff22"><label>22</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2176 4817</institution-id><institution-id institution-id-type="GRID">grid.5399.6</institution-id><institution></institution><institution>CNRS, Aix-Marseille Université,</institution></institution-wrap>Marseille, France</aff><aff id="Aff23"><label>23</label><institution-wrap><institution-id institution-id-type="GRID">grid.418532.9</institution-id><institution></institution><institution>Institut Pasteur de Montevideo, Unidad Mixta INIA-IPMont,</institution></institution-wrap>Mataojo 2020, CP11400 Montevideo, Uruguay</aff><aff id="Aff24"><label>24</label>INRA, USC 1408 AFMB, 13288 Marseille, France</aff><aff id="Aff25"><label>25</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0619 1117</institution-id><institution-id institution-id-type="GRID">grid.412125.1</institution-id><institution>Department of Biological Sciences,</institution><institution>King Abdulaziz University,</institution></institution-wrap>Jeddah, Saudi Arabia</aff><aff id="Aff26"><label>26</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0410 2071</institution-id><institution-id institution-id-type="GRID">grid.7737.4</institution-id><institution>Department of Food and Environmental Sciences,</institution><institution>University of Helsinki,</institution></institution-wrap>Viikinkaari 9, Helsinki, Finland</aff><aff id="Aff27"><label>27</label>Dutch DNA Biotech BV, Utrechtseweg 48, 3703AJ Zeist, The Netherlands</aff><aff id="Aff28"><label>28</label><institution-wrap><institution-id institution-id-type="ISNI">0000000084992262</institution-id><institution-id institution-id-type="GRID">grid.7177.6</institution-id><institution></institution><institution>Swammerdam Institute for Life Sciences, University of Amsterdam,</institution></institution-wrap>Amsterdam, The Netherlands</aff><aff id="Aff29"><label>29</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0721 1626</institution-id><institution-id institution-id-type="GRID">grid.11914.3c</institution-id><institution>School of Biology,</institution><institution>University of St Andrews,</institution></institution-wrap>St Andrews, Fife KY16 9TH UK</aff><aff id="Aff30"><label>30</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Department of Medicine, Faculty of Medicine,</institution><institution>University of Debrecen,</institution></institution-wrap>Nagyerdei krt. 98, 4032 Debrecen, Hungary</aff><aff id="Aff31"><label>31</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0482 5331</institution-id><institution-id institution-id-type="GRID">grid.411984.1</institution-id><institution>Department of Medical Informatics,</institution><institution>University Medical Centre,</institution></institution-wrap>Robert-Koch-Str.40, 37075 Göttingen, Germany</aff><aff id="Aff32"><label>32</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0482 5331</institution-id><institution-id institution-id-type="GRID">grid.411984.1</institution-id><institution>Department of Molecular Biology,</institution><institution>Universitätsmedizin Göttingen,</institution></institution-wrap>Humboldtallee 23, Göttingen, 37073 Germany</aff><aff id="Aff33"><label>33</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2176 4817</institution-id><institution-id institution-id-type="GRID">grid.5399.6</institution-id><institution></institution><institution>INRA, Aix-Marseille Univ, BBF, Biodiversité et Biotechnologie Fongiques,</institution></institution-wrap>Marseille, France</aff><aff id="Aff34"><label>34</label><institution-wrap><institution-id institution-id-type="GRID">grid.473653.0</institution-id><institution></institution><institution>Institute of Sciences of Food Production (ISPA), National Research Council (CNR),</institution></institution-wrap>Via Amendola 122/O, 70126 Bari, Italy</aff><aff id="Aff35"><label>35</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1945 7738</institution-id><institution-id institution-id-type="GRID">grid.419051.8</institution-id><institution>Departamento de Biotecnología,</institution><institution>Instituto de Agroquímica y Tecnología de Alimentos, Consejo Superior de Investigaciones Científicas (CSIC),</institution></institution-wrap>Paterna, Valencia, Spain</aff><aff id="Aff36"><label>36</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2163 588X</institution-id><institution-id institution-id-type="GRID">grid.411247.5</institution-id><institution>Departamento de Genética e Evolução,</institution><institution>Centro de Ciências Biológicas e da Saúde, Universidade Federal de São Carlos,</institution></institution-wrap>São Carlos, São Paulo Brazil</aff><aff id="Aff37"><label>37</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0000 8578 2742</institution-id><institution-id institution-id-type="GRID">grid.6341.0</institution-id><institution>Uppsala BioCenter, Department of Microbiology,</institution><institution>Swedish University of Agricultural Sciences,</institution></institution-wrap>P.O. Box 7025, 750 07 Uppsala, Sweden</aff><aff id="Aff38"><label>38</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2292 8254</institution-id><institution-id institution-id-type="GRID">grid.6734.6</institution-id><institution>Institute of Biotechnology, Department Applied and Molecular Microbiology,</institution><institution>Berlin University of Technology,</institution></institution-wrap>Gustav-Meyer-Allee 25, 13355 Berlin, Germany</aff><aff id="Aff39"><label>39</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>MTA-DE Momentum, Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology,</institution><institution>University of Debrecen,</institution></institution-wrap>Nagyerdei krt.98., 4032 Debrecen, Hungary</aff><aff id="Aff40"><label>40</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0661 1556</institution-id><institution-id institution-id-type="GRID">grid.258803.4</institution-id><institution></institution><institution>School of Food Science and Biotechnology, Kyungpook National University,</institution></institution-wrap>Daegu, 702-701 Republic of Korea</aff><aff id="Aff41"><label>41</label><institution-wrap><institution-id institution-id-type="ISNI">0000000121657640</institution-id><institution-id institution-id-type="GRID">grid.11630.35</institution-id><institution>Sección Bioquímica, Departamento de Biología Celular y Molecular, Facultad de Ciencias,</institution><institution>Universidad de la República,</institution></institution-wrap>Montevideo, Uruguay</aff><aff id="Aff42"><label>42</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0075 5874</institution-id><institution-id institution-id-type="GRID">grid.7892.4</institution-id><institution>Department of Microbiology,</institution><institution>Karlsruhe Institute of Technology, Institute for Applied Biosciences,</institution></institution-wrap>Hertzstrasse 16,, 76187 Karlsruhe, Germany</aff><aff id="Aff43"><label>43</label>Department of Biology, School of Science, University of Sulaimani, Al Sulaymaneyah, Iraq</aff><aff id="Aff44"><label>44</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1088 8582</institution-id><institution-id institution-id-type="GRID">grid.7122.6</institution-id><institution>Institute of Food Science, Faculty of Agricultural and Food Sciences and Environmental Management,</institution><institution>University of Debrecen,</institution></institution-wrap>4032 Debrecen, Hungary</aff><aff id="Aff45"><label>45</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0721 6013</institution-id><institution-id institution-id-type="GRID">grid.8954.0</institution-id><institution>Department of Biology, Biotechnical Faculty,</institution><institution>University of Ljubljana,</institution></institution-wrap>Jamnikarjeva 101, 1000 Ljubljana, Slovenia</aff><aff id="Aff46"><label>46</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0143 807X</institution-id><institution-id institution-id-type="GRID">grid.418398.f</institution-id><institution></institution><institution>Systems Biology/Bioinformatics group, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knoell Institute, (HKI),</institution></institution-wrap>Beutenbergstr. 11a, 07745 Jena, Germany</aff><aff id="Aff47"><label>47</label><institution-wrap><institution-id institution-id-type="ISNI">0000000419368956</institution-id><institution-id institution-id-type="GRID">grid.168010.e</institution-id><institution>Department of Genetics,</institution><institution>Stanford University,</institution></institution-wrap>Stanford, CA 94305-5120 USA</aff><aff id="Aff48"><label>48</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0737 1259</institution-id><institution-id institution-id-type="GRID">grid.36567.31</institution-id><institution>Department of Plant Pathology,</institution><institution>Kansas State University,</institution></institution-wrap>Manhattan, KS 66506 USA</aff><aff id="Aff49"><label>49</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8630</institution-id><institution-id institution-id-type="GRID">grid.410319.e</institution-id><institution></institution><institution>Centre for Structural and Functional Genomics, Concordia University,</institution></institution-wrap>7141 Sherbrooke Street West, Montreal, QC H4B 1R6 Canada</aff><aff id="Aff50"><label>50</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2181 8870</institution-id><institution-id institution-id-type="GRID">grid.5170.3</institution-id><institution>Department of Biotechnology and Biomedicine,</institution><institution>Technical University of Denmark,</institution></institution-wrap>Søltofts Plads 223, 2800 Kongens Lyngby, Denmark</aff><aff id="Aff51"><label>51</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2167 3675</institution-id><institution-id institution-id-type="GRID">grid.14003.36</institution-id><institution>Departments of Bacteriology and Genetics,</institution><institution>University of Wisconsin-Madison,</institution></institution-wrap>1550 Linden Drive, Madison, WI 53706 USA</aff><aff id="Aff52"><label>52</label>Fungal Biotechnology Team, Pacific Northwest National Laboratory, Richland, Washington, 99352 USA</aff><aff id="Aff53"><label>53</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1939 2794</institution-id><institution-id institution-id-type="GRID">grid.9613.d</institution-id><institution>Department of Molecular and Applied Microbiology,</institution><institution>Leibniz-Institute for Natural Product Research and Infection Biology - Hans Knoell Institute (HKI) and Institute for Microbiology, Friedrich Schiller University Jena,</institution></institution-wrap>Beutenbergstr. 11a, 07745 Jena, Germany</aff><aff id="Aff54"><label>54</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1937 0722</institution-id><institution-id institution-id-type="GRID">grid.11899.38</institution-id><institution>Faculdade de Ciências Farmacêuticas de Ribeirão Preto,</institution><institution>Universidade de São Paulo,</institution></institution-wrap>Av. do Café S/N, CEP 14040-903 Ribeirão Preto, São Paulo Brazil</aff><aff id="Aff55"><label>55</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2106 0692</institution-id><institution-id institution-id-type="GRID">grid.266515.3</institution-id><institution>Department of Molecular Biosciences,</institution><institution>University of Kansas,</institution></institution-wrap>Lawrence, Kansas 66045 USA</aff><aff id="Aff56"><label>56</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2113 8111</institution-id><institution-id institution-id-type="GRID">grid.7445.2</institution-id><institution>Department of Microbiology,</institution><institution>Imperial College,</institution></institution-wrap>London, SW7 2AZ UK</aff><aff id="Aff57"><label>57</label>Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris‐Sud, Université Paris‐Saclay, 91198 Gif‐sur‐Yvette cedex, France</aff><aff id="Aff58"><label>58</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2348 4034</institution-id><institution-id institution-id-type="GRID">grid.5329.d</institution-id><institution>Research Division Biochemical Technology,</institution><institution>Institute of Chemical Engineering, TU Wien,</institution></institution-wrap>Gumpendorferstraße 1a, 1060 Vienna, Austria</aff><aff id="Aff59"><label>59</label><institution-wrap><institution-id institution-id-type="GRID">grid.66859.34</institution-id><institution></institution><institution>Broad Institute,</institution></institution-wrap>415 Main St, Cambridge, MA 02142 USA</aff><aff id="Aff60"><label>60</label>Present address: VTT Brasil, Alameda Inajá, 123, CEP 06460-055 Barueri, São Paulo Brazil</aff><aff id="Aff61"><label>61</label><institution-wrap><institution-id institution-id-type="GRID">grid.431777.1</institution-id><institution></institution><institution>Present address: CSIRO Publishing,</institution></institution-wrap>Unipark, Building 1 Level 1, 195 Wellington Road, Clayton, VIC 3168 Australia</aff><aff id="Aff62"><label>62</label>Present address: Université Libre de Bruxelles Institute of Molecular Biology and Medicine (IBMM), Brussels, Belgium</aff><aff id="Aff63"><label>63</label>Present address: Instituto de Profesores Artigas, Consejo de Formación en Educación, ANEP, CP 11800, Av. del Libertador 2025, Montevideo, Uruguay</aff><aff id="Aff64"><label>64</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2108 7481</institution-id><institution-id institution-id-type="GRID">grid.9594.1</institution-id><institution>Present Address: Department of Chemistry,</institution><institution>University of Ioannina,</institution></institution-wrap>Ioannina, 45110 Greece</aff><aff id="Aff65"><label>65</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2289 6897</institution-id><institution-id institution-id-type="GRID">grid.15447.33</institution-id><institution></institution><institution>Present address: Center for Algorithmic Biotechnology, St.Petersburg State University,</institution></institution-wrap>St. Petersburg, Russia</aff><aff id="Aff66"><label>66</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0407 1584</institution-id><institution-id institution-id-type="GRID">grid.414336.7</institution-id><institution></institution><institution>Present address: Aix-Marseille Université, Unité de Recherche sur les Maladies Infectieuses et Tropicales Emergentes (URMITE), UM63, CNRS 7278, IRD 198, INSERM U1095, IHU Méditerranée Infection, Pôle des Maladies Infectieuses, Assistance Publique-Hôpitaux de Marseille, Faculté de Médecine,</institution></institution-wrap>27 Bd Jean Moulin, 13005 Marseille, France</aff><aff id="Aff67"><label>67</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 1523 2072</institution-id><institution-id institution-id-type="GRID">grid.437386.d</institution-id><institution></institution><institution>Present address: Swedish Chemicals Agency,</institution></institution-wrap>Box 2, 172 13 Sundbyberg, Sweden</aff><aff id="Aff68"><label>68</label>Present address: Instituto de Ciencia y Tecnología Dr. César Milstein, Fundación Pablo Cassará, CONICET, Saladillo 2468 C1440FFX, Ciudad de Buenos Aires, Argentina</aff><aff id="Aff69"><label>69</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8630</institution-id><institution-id institution-id-type="GRID">grid.410319.e</institution-id><institution></institution><institution>Present address: Centre for Structural and Functional Genomics, Concordia University,</institution></institution-wrap>7141 Sherbrooke Street West, Montreal, QC H4B 1R6 Canada</aff><aff id="Aff70"><label>70</label>Present address: INRA UMR1198 Biologie du Développement et de la Reproduction - Domaine de Vilvert, Jouy en Josas, 78352 Cedex France</aff><aff id="Aff71"><label>71</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 2292 8254</institution-id><institution-id institution-id-type="GRID">grid.6734.6</institution-id><institution>Present address: Department Applied and Molecular Microbiology,</institution><institution>Institute of Biotechnology, Berlin University of Technology,</institution></institution-wrap>Gustav-Meyer-Allee 25, 13355 Berlin, Germany</aff><aff id="Aff72"><label>72</label>Present address: BaseClear B.V., Einsteinweg 5, 2333 CC Leiden, The Netherlands</aff><aff id="Aff73"><label>73</label>Present address: Seres Therapeutics, 200 Sidney St, Cambridge, MA 02139 USA</aff><aff id="Aff74"><label>74</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 1936 8630</institution-id><institution-id institution-id-type="GRID">grid.410319.e</institution-id><institution></institution><institution>Present address: Centre of Functional and Structure Genomics Biology Department Concordia University,</institution></institution-wrap>7141 Sherbrooke St. W., Montreal, QC H4B 1R6 Canada</aff></contrib-group><pub-date pub-type="epub"><day>14</day><month>2</month><year>2017</year></pub-date><pub-date pub-type="pmc-release"><day>14</day><month>2</month><year>2017</year></pub-date><pub-date pub-type="collection"><year>2017</year></pub-date><volume>18</volume><elocation-id>28</elocation-id><history><date date-type="received"><day>5</day><month>7</month><year>2016</year></date><date date-type="accepted"><day>10</day><month>1</month><year>2017</year></date></history><permissions><copyright-statement>© The Author(s). 2017</copyright-statement><license license-type="OpenAccess"><license-p><bold>Open Access</bold>This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/4.0/">http://creativecommons.org/licenses/by/4.0/</ext-link>), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/publicdomain/zero/1.0/">http://creativecommons.org/publicdomain/zero/1.0/</ext-link>) applies to the data made available in this article, unless otherwise stated.</license-p></license></permissions><abstract id="Abs1"><sec><title>Background</title><p>The fungal genus <italic>Aspergillus</italic> is of critical importance to humankind. Species include those with industrial applications, important pathogens of humans, animals and crops, a source of potent carcinogenic contaminants of food, and an important genetic model. The genome sequences of eight aspergilli have already been explored to investigate aspects of fungal biology, raising questions about evolution and specialization within this genus.</p></sec><sec><title>Results</title><p>We have generated genome sequences for ten novel, highly diverse <italic>Aspergillus</italic> species and compared these in detail to sister and more distant genera. Comparative studies of key aspects of fungal biology, including primary and secondary metabolism, stress response, biomass degradation, and signal transduction, revealed both conservation and diversity among the species. Observed genomic differences were validated with experimental studies. This revealed several highlights, such as the potential for sex in asexual species, organic acid production genes being a key feature of black aspergilli, alternative approaches for degrading plant biomass, and indications for the genetic basis of stress response. A genome-wide phylogenetic analysis demonstrated in detail the relationship of the newly genome sequenced species with other aspergilli.</p></sec><sec><title>Conclusions</title><p>Many aspects of biological differences between fungal species cannot be explained by current knowledge obtained from genome sequences. The comparative genomics and experimental study, presented here, allows for the first time a genus-wide view of the biological diversity of the aspergilli and in many, but not all, cases linked genome differences to phenotype. Insights gained could be exploited for biotechnological and medical applications of fungi.</p></sec><sec><title>Electronic supplementary material</title><p>The online version of this article (doi:10.1186/s13059-017-1151-0) contains supplementary material, which is available to authorized users.</p></sec></abstract><kwd-group xml:lang="en"><title>Keywords</title><kwd><italic>Aspergillus</italic></kwd><kwd>Genome sequencing</kwd><kwd>Comparative genomics</kwd><kwd>Fungal biology</kwd></kwd-group><funding-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100003549</institution-id><institution>Országos Tudományos Kutatási Alapprogramok</institution></institution-wrap></funding-source><award-id>K100464</award-id><award-id>NN116519</award-id><principal-award-recipient><name><surname>Karaffa</surname><given-names>Levente</given-names></name><name><surname>Pócsi</surname><given-names>István</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100002347</institution-id><institution>Bundesministerium für Bildung und Forschung</institution></institution-wrap></funding-source></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100001659</institution-id><institution>Deutsche Forschungsgemeinschaft</institution></institution-wrap></funding-source><award-id>FOR1334/2</award-id><award-id>FOR1334/2</award-id><principal-award-recipient><name><surname>Fischer</surname><given-names>Reinhard</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100001809</institution-id><institution>National Natural Science Foundation of China</institution></institution-wrap></funding-source><award-id>31330059</award-id><principal-award-recipient><name><surname>Chen</surname><given-names>Fusheng</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100002338</institution-id><institution>Ministry of Education of the People's Republic of China</institution></institution-wrap></funding-source><award-id>2662014BQ051</award-id><award-id>2662015QC003</award-id><principal-award-recipient><name><surname>Chen</surname><given-names>Wanping</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100003958</institution-id><institution>Stichting voor de Technische Wetenschappen</institution></institution-wrap></funding-source><award-id>UGC 14270</award-id><award-id>LGC 7393</award-id><principal-award-recipient><name><surname>de Vries</surname><given-names>Ronald P.</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution>Austrian Science Fund (AT)</institution></funding-source><award-id>M01693-B22</award-id><principal-award-recipient><name><surname>Cánovas</surname><given-names>David</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100004085</institution-id><institution>Ministry of Education, Science and Technology </institution></institution-wrap></funding-source><award-id>2011-0031955</award-id><principal-award-recipient><name><surname>Bayram</surname><given-names>Özgür</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100001602</institution-id><institution>Science Foundation Ireland</institution></institution-wrap></funding-source><award-id>13/CDA/2142</award-id><principal-award-recipient><name><surname>Bayram</surname><given-names>Özgür</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution>Kurdistan Regional Government of Iraq</institution></funding-source></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/100009689</institution-id><institution>British Mycological Society</institution></institution-wrap></funding-source></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100000268</institution-id><institution>Biotechnology and Biological Sciences Research Council</institution></institution-wrap></funding-source></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/100004322</institution-id><institution>Agilent Technologies</institution></institution-wrap></funding-source><award-id>#2871</award-id></award-group><award-group><funding-source><institution>Novo Nordisk Foundation</institution></funding-source><award-id>13OC0005201</award-id></award-group><award-group><funding-source><institution>MINECO/FEDER</institution></funding-source><award-id>AGL2011-29925</award-id><award-id>AGL2015-66131- AGL2015-66131-C2-2-R</award-id><principal-award-recipient><name><surname>Orejas</surname><given-names>Margarita</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution>Irving S. Johnson fund</institution></funding-source></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100001807</institution-id><institution>Fundação de Amparo à Pesquisa do Estado de São Paulo</institution></institution-wrap></funding-source><award-id>2012/19040-0</award-id><award-id>2014/10351-8</award-id><principal-award-recipient><name><surname>Uchima</surname><given-names>Cristiane Akemi</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution>CNPq</institution></funding-source><award-id>442333/2014-5</award-id><award-id>441912/2014-1</award-id><principal-award-recipient><name><surname>Damásio</surname><given-names>André Ricardo de Lima</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution>Dirección General de Apoyo al Personal Académico</institution></funding-source><award-id>IN 225710</award-id><award-id>IN219813</award-id><principal-award-recipient><name><surname>Aguilar-Osorio</surname><given-names>Guillermo</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution>Slovenian Research Agency</institution></funding-source><award-id>P1-0391</award-id><award-id>J4-7162</award-id><principal-award-recipient><name><surname>Kraševec</surname><given-names>Nada</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100003621</institution-id><institution>Ministry of Science, ICT and Future Planning</institution></institution-wrap></funding-source><award-id>2011-0031955</award-id><principal-award-recipient><name><surname>Yu</surname><given-names>Jae-Hyuk</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/100000015</institution-id><institution>U.S. Department of Energy</institution></institution-wrap></funding-source><award-id>DE-AC02-05CH11231</award-id><principal-award-recipient><name><surname>de Vries</surname><given-names>Ronald P.</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/100008398</institution-id><institution>Villum Fonden</institution></institution-wrap></funding-source><award-id>VKR023437</award-id><award-id>VKR023437</award-id></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100004285</institution-id><institution>Saint Petersburg State University</institution></institution-wrap></funding-source><award-id>15.61.951.2015</award-id><principal-award-recipient><name><surname>Lapidus</surname><given-names>Alla</given-names></name></principal-award-recipient></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100001807</institution-id><institution>Fundação de Amparo à Pesquisa do Estado de São Paulo</institution></institution-wrap></funding-source></award-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">http://dx.doi.org/10.13039/501100003593</institution-id><institution>Conselho Nacional de Desenvolvimento Científico e Tecnológico</institution></institution-wrap></funding-source></award-group></funding-group><custom-meta-group><custom-meta><meta-name>issue-copyright-statement</meta-name><meta-value>© The Author(s) 2017</meta-value></custom-meta></custom-meta-group></article-meta></front><body><sec id="Sec1"><title>Background</title><p>The genus <italic>Aspergillus</italic> is one of the best studied genera of filamentous fungi, largely because of the medical (<italic>A. fumigatus</italic>, <italic>A. terreus</italic>), food spoilage (<italic>A. flavus</italic>, <italic>A. parasiticus</italic>), and industrial (<italic>A. niger</italic>, <italic>A. aculeatus</italic>, <italic>A. oryzae</italic>) relevance of some of its species, in addition to the fundamental studies in the model fungus <italic>A. nidulans</italic> that have contributed broadly to our understanding of eukaryotic cell biology and molecular processes. Aspergilli can grow in a wide range of niches, mainly in soils and on dead matter, and some are also capable of colonizing living animal or plant hosts and, in total, approximately 350 species have been identified in this genus [<xref ref-type="bibr" rid="CR1">1</xref>]. The broad relevance and economic importance of the genus has pushed it to the forefront of fungal research, with one of the largest academic and industrial research communities [<xref ref-type="bibr" rid="CR2">2</xref>].</p><p><italic>Aspergillus</italic> species are characterized by the unifying feature of the “aspergillum,” an asexual reproductive structure. The aspergilli form a broad monophyletic group, but show large taxonomic divergence with respect to morphology [<xref ref-type="bibr" rid="CR3">3</xref>] and phylogenetic distance [<xref ref-type="bibr" rid="CR4">4</xref>]. Genome sequences for three aspergilli [<xref ref-type="bibr" rid="CR4">4</xref>–<xref ref-type="bibr" rid="CR6">6</xref>] were among the first to be reported from filamentous fungi and were soon followed by an additional five genomes [<xref ref-type="bibr" rid="CR7">7</xref>–<xref ref-type="bibr" rid="CR10">10</xref>]. This has resulted in many genomic, comparative genomic, and post-genomic studies covering a wide variety of topics [<xref ref-type="bibr" rid="CR11">11</xref>, <xref ref-type="bibr" rid="CR12">12</xref>], largely due to the size of the <italic>Aspergillus</italic> research community. These studies were facilitated by genome resources for this genus, such as CADRE [<xref ref-type="bibr" rid="CR13">13</xref>] and AspGD [<xref ref-type="bibr" rid="CR14">14</xref>], in which gene curation and functional annotation of reference species were combined with synteny and orthology analysis. The inclusion of these genomes in MycoCosm [<xref ref-type="bibr" rid="CR15">15</xref>, <xref ref-type="bibr" rid="CR16">16</xref>] enabled comparison to sister and more distant genera. These studies also revealed substantial genomic variations between these species and raised questions about the evolution of various aspects of fungal biology within the genus.</p><p>In this study, ten novel genome sequences of the genus <italic>Aspergillus</italic> were generated, namely <italic>A. luchuensis</italic>, <italic>A. aculeatus</italic>, <italic>A. brasiliensis</italic>, <italic>A. carbonarius</italic>, <italic>A. glaucus</italic>, <italic>A. sydowii</italic>, <italic>A. tubingensis</italic>, <italic>A. versicolor</italic>, <italic>A. wentii</italic>, and <italic>A. zonatus</italic>. These species were chosen primarily to provide better coverage of the whole genus, to complement the already available genome sequences of <italic>A. clavatus</italic>, <italic>A. fischeri</italic>, <italic>A. flavus</italic>, <italic>A. fumigatus</italic>, <italic>A. nidulans</italic>, <italic>A. niger</italic>, <italic>A. oryzae</italic>, and <italic>A. terreus</italic>, and to allow more detailed data mining of the industrially relevant section <italic>Nigri</italic> (<italic>A. luchuensis</italic>, <italic>A. aculeatus</italic>, <italic>A. brasiliensis</italic>, <italic>A. carbonarius</italic>, <italic>A. niger</italic>, <italic>A. tubingensis</italic>). Additional species from the section <italic>Nidulantes</italic> were included because of the high divergence of the genome sequence of <italic>A. nidulans</italic> from the other <italic>Aspergillus</italic> genomes, and <italic>A. sydowii</italic> because of its marine life-style and being a pathogen of Gorgonian corals [<xref ref-type="bibr" rid="CR17">17</xref>]. We demonstrate that this combined set of genomes provides a highly valuable dataset for comparative and functional genomics. This study was performed as a global consortium effort with different researchers addressing different topics as subgroups of the consortium. Where possible, experimental data were generated to examine inferences from the genomic differences and to provide an unprecedented comparative analysis of variation and functional specialization within a fungal genus. The paper is organized in topic based sections, covering:<list list-type="bullet"><list-item><p>General comparison of the genomes and phylogenomics</p></list-item><list-item><p>Asexual and sexual reproduction</p></list-item><list-item><p>Primary carbon catabolism</p></list-item><list-item><p>Plant biomass degradation</p></list-item><list-item><p>Secondary metabolism</p></list-item><list-item><p>Stress response</p></list-item><list-item><p>Transporters</p></list-item><list-item><p>Flavohemoglobins and nitric oxide sensitivity</p></list-item><list-item><p>Signal transduction pathway genes</p></list-item><list-item><p>DNA protein organisation and methylation</p></list-item></list></p></sec><sec id="Sec2" sec-type="discussion"><title>Results and discussion</title><sec id="Sec3"><title>General comparison of the genomes and phylogenomics</title><p>The genome sequences were generated at the Joint Genome Institute (JGI) and compared to other fungal genomes in JGI’s MycoCosm database [<xref ref-type="bibr" rid="CR15">15</xref>] with respect to genome size, structure, and gene content (Table <xref rid="Tab1" ref-type="table">1</xref>, Fig. <xref rid="Fig1" ref-type="fig">1</xref>, Additional file <xref rid="MOESM1" ref-type="media">1</xref>). All <italic>Aspergillus</italic> genomes are similar in size (29–36 Mb) and GC content (48–53%), while smaller genomes are present in the Onygenales (Table <xref rid="Tab1" ref-type="table">1</xref>, Additional file <xref rid="MOESM1" ref-type="media">1</xref>A). The number of predicted genes in the aspergilli is in the range of 9113–13,553, which is generally higher than that observed for the Onygenales (<10,000; Additional file <xref rid="MOESM1" ref-type="media">1</xref>B). Larger differences were found for the repetitive portion of the genome, which is in the range of 100 kb to 1.3 Mb for the aspergilli. Genomes of the Aspergillaceae have an average repeat content of 2–3% (Additional file <xref rid="MOESM1" ref-type="media">1</xref>C).<table-wrap id="Tab1"><label>Table 1</label><caption><p>Comparison of genome features of 34 ascomycete genomes</p></caption><table frame="hsides" rules="groups"><thead><tr><th>Species</th><th>Strain</th><th>Class</th><th>Order</th><th>Section</th><th>Genome size (Mb)</th><th>GC %</th><th>Contigs (<italic>n</italic>)</th><th>Reference</th></tr></thead><tbody><tr><td><italic>Aspergillus niger</italic></td><td>ATCC1015</td><td>Eurotiomycetes</td><td>Eurotiales</td><td><italic>Nigri</italic></td><td>35</td><td char="." align="char">50.3</td><td>24</td><td>[<xref ref-type="bibr" rid="CR7">7</xref>]</td></tr><tr><td><italic>Aspergillus niger</italic></td><td>CBS513.88</td><td>Eurotiomycetes</td><td>Eurotiales</td><td><italic>Nigri</italic></td><td>34</td><td char="." align="char">50.5</td><td>470</td><td>[<xref ref-type="bibr" rid="CR10">10</xref>]</td></tr><tr><td><bold><italic>Aspergillus luchuensis</italic></bold></td><td><bold>CBS106.47</bold></td><td><bold>Eurotiomycetes</bold></td><td><bold>Eurotiales</bold></td><td><bold><italic>Nigri</italic></bold></td><td><bold>37</bold></td><td char="." align="char"><bold>49.1</bold></td><td><bold>318</bold></td><td><bold>This study</bold></td></tr><tr><td><bold><italic>Aspergillus tubingensis</italic></bold></td><td><bold>CBS134.48</bold></td><td><bold>Eurotiomycetes</bold></td><td><bold>Eurotiales</bold></td><td><bold><italic>Nigri</italic></bold></td><td><bold>35</bold></td><td char="." align="char"><bold>49.2</bold></td><td><bold>87</bold></td><td><bold>This study</bold></td></tr><tr><td><bold><italic>Aspergillus brasiliensis</italic></bold></td><td><bold>CBS101740</bold></td><td><bold>Eurotiomycetes</bold></td><td><bold>Eurotiales</bold></td><td><bold><italic>Nigri</italic></bold></td><td><bold>36</bold></td><td char="." align="char"><bold>50.5</bold></td><td><bold>290</bold></td><td><bold>This study</bold></td></tr><tr><td><bold><italic>Aspergillus carbonarius</italic></bold></td><td><bold>CBS141172</bold></td><td><bold>Eurotiomycetes</bold></td><td><bold>Eurotiales</bold></td><td><bold><italic>Nigri</italic></bold></td><td><bold>36</bold></td><td char="." align="char"><bold>51.7</bold></td><td><bold>1346</bold></td><td><bold>This study</bold></td></tr><tr><td><bold><italic>Aspergillus aculeatus</italic></bold></td><td><bold>CBS172.66</bold></td><td><bold>Eurotiomycetes</bold></td><td><bold>Eurotiales</bold></td><td><bold><italic>Nigri</italic></bold></td><td><bold>35</bold></td><td char="." align="char"><bold>50.9</bold></td><td><bold>851</bold></td><td><bold>This study</bold></td></tr><tr><td><bold><italic>Aspergillus versicolor</italic></bold></td><td><bold>CBS795.97</bold></td><td><bold>Eurotiomycetes</bold></td><td><bold>Eurotiales</bold></td><td><bold><italic>Nidulantes</italic></bold></td><td><bold>33</bold></td><td char="." align="char"><bold>50.1</bold></td><td><bold>58</bold></td><td><bold>This study</bold></td></tr><tr><td><bold><italic>Aspergillus sydowii</italic></bold></td><td><bold>CBS593.65</bold></td><td><bold>Eurotiomycetes</bold></td><td><bold>Eurotiales</bold></td><td><bold><italic>Nidulantes</italic></bold></td><td><bold>34</bold></td><td char="." align="char"><bold>50.0</bold></td><td><bold>133</bold></td><td><bold>This study</bold></td></tr><tr><td><italic>Aspergillus nidulans</italic></td><td>FGSC A4</td><td>Eurotiomycetes</td><td>Eurotiales</td><td><italic>Nidulantes</italic></td><td>30</td><td char="." align="char">50.4</td><td>82</td><td>[<xref ref-type="bibr" rid="CR4">4</xref>]</td></tr><tr><td><italic>Aspergillus flavus</italic></td><td>NRRL3557</td><td>Eurotiomycetes</td><td>Eurotiales</td><td><italic>Flavi</italic></td><td>37</td><td char="." align="char">48.4</td><td>765</td><td>[<xref ref-type="bibr" rid="CR9">9</xref>]</td></tr><tr><td><italic>Aspergillus oryzae</italic></td><td>RIB40</td><td>Eurotiomycetes</td><td>Eurotiales</td><td><italic>Flavi</italic></td><td>38</td><td char="." align="char">48.3</td><td>28</td><td>[<xref ref-type="bibr" rid="CR5">5</xref>]</td></tr><tr><td><italic>Aspergillus terreus</italic></td><td>NIH2624</td><td>Eurotiomycetes</td><td>Eurotiales</td><td><italic>Terrei</italic></td><td>29</td><td char="." align="char">52.9</td><td>267</td><td>[<xref ref-type="bibr" rid="CR14">14</xref>]</td></tr><tr><td><italic>Aspergillus fumigatus</italic></td><td>Af293</td><td>Eurotiomycetes</td><td>Eurotiales</td><td><italic>Fumigati</italic></td><td>29</td><td char="." align="char">49.8</td><td>19</td><td>[<xref ref-type="bibr" rid="CR6">6</xref>]</td></tr><tr><td><italic>Aspergillus fischeri</italic></td><td>NRRL181</td><td>Eurotiomycetes</td><td>Eurotiales</td><td><italic>Fumigati</italic></td><td>33</td><td char="." align="char">49.4</td><td>976</td><td>[<xref ref-type="bibr" rid="CR8">8</xref>]</td></tr><tr><td><italic>Aspergillus clavatus</italic></td><td>NRRL1</td><td>Eurotiomycetes</td><td>Eurotiales</td><td><italic>Clavati</italic></td><td>28</td><td char="." align="char">49.2</td><td>143</td><td>[<xref ref-type="bibr" rid="CR8">8</xref>]</td></tr><tr><td><bold><italic>Aspergillus glaucus</italic></bold></td><td><bold>CBS516.65</bold></td><td><bold>Eurotiomycetes</bold></td><td><bold>Eurotiales</bold></td><td><bold><italic>Aspergillus</italic></bold></td><td><bold>30</bold></td><td char="." align="char"><bold>49.4</bold></td><td><bold>433</bold></td><td><bold>This study</bold></td></tr><tr><td><bold><italic>Aspergillus wentii</italic></bold></td><td><bold>CBS141173</bold></td><td><bold>Eurotiomycetes</bold></td><td><bold>Eurotiales</bold></td><td><bold><italic>Cremei</italic></bold></td><td><bold>31</bold></td><td char="." align="char"><bold>48.0</bold></td><td><bold>118</bold></td><td><bold>This study</bold></td></tr><tr><td><bold><italic>Penicillium chrysogenum</italic></bold></td><td><bold>unknown</bold></td><td><bold>Eurotiomycetes</bold></td><td><bold>Eurotiales</bold></td><td><bold><italic>Chrysogena</italic></bold></td><td><bold>31</bold></td><td char="." align="char"><bold>48.8</bold></td><td><bold>299</bold></td><td><bold>This study</bold></td></tr><tr><td><italic>Penicillium rubens</italic></td><td>Wisconsin 54-1255</td><td>Eurotiomycetes</td><td>Eurotiales</td><td><italic>Chrysogena</italic></td><td>32</td><td char="." align="char">49.0</td><td>242</td><td>[<xref ref-type="bibr" rid="CR18">18</xref>]</td></tr><tr><td><italic>Penicillium digitatum</italic></td><td>PHI26</td><td>Eurotiomycetes</td><td>Eurotiales</td><td><italic>Penicillium</italic></td><td>26</td><td char="." align="char">48.9</td><td>304</td><td>[<xref ref-type="bibr" rid="CR19">19</xref>]</td></tr><tr><td><bold><italic>Aspergillus zonatus</italic></bold></td><td><bold>CBS506.65</bold></td><td><bold>Eurotiomycetes</bold></td><td><bold>Eurotiales</bold></td><td><bold>Unclassified</bold></td><td><bold>29</bold></td><td char="." align="char"><bold>48.3</bold></td><td><bold>460</bold></td><td><bold>This study</bold></td></tr><tr><td><italic>Talaromyces marneffei</italic></td><td>ATCC18224</td><td>Eurotiomycetes</td><td>Eurotiales</td><td><italic>Talaromyces</italic></td><td>29</td><td char="." align="char">46.7</td><td>524</td><td>Unpublished</td></tr><tr><td><italic>Talaromyces stipitatus</italic></td><td>ATCC10500</td><td>Eurotiomycetes</td><td>Eurotiales</td><td><italic>Talaromyces</italic></td><td>36</td><td char="." align="char">46.1</td><td>896</td><td>Unpublished</td></tr><tr><td><italic>Coccidioides immitis</italic></td><td>RS</td><td>Eurotiomycetes</td><td>Onygenales</td><td></td><td>29</td><td char="." align="char">46.0</td><td>10</td><td>[<xref ref-type="bibr" rid="CR20">20</xref>]</td></tr><tr><td><italic>Coccidioides posadasii</italic></td><td>C735 delta SOWgp</td><td>Eurotiomycetes</td><td>Onygenales</td><td></td><td>27</td><td char="." align="char">46.6</td><td>55</td><td>[<xref ref-type="bibr" rid="CR20">20</xref>]</td></tr><tr><td><italic>Uncinocarpus reesii</italic></td><td>1704</td><td>Eurotiomycetes</td><td>Onygenales</td><td></td><td>22</td><td char="." align="char">48.7</td><td>582</td><td>[<xref ref-type="bibr" rid="CR20">20</xref>]</td></tr><tr><td><italic>Microsporum canis</italic></td><td>CBS113480</td><td>Eurotiomycetes</td><td>Onygenales</td><td></td><td>23</td><td char="." align="char">47.5</td><td>309</td><td>[<xref ref-type="bibr" rid="CR21">21</xref>]</td></tr><tr><td><italic>Trichophyton rubrum</italic></td><td>CBS118892</td><td>Eurotiomycetes</td><td>Onygenales</td><td></td><td>23</td><td char="." align="char">48.3</td><td>622</td><td>[<xref ref-type="bibr" rid="CR21">21</xref>]</td></tr><tr><td><italic>Histoplasma capsulatum</italic></td><td>NAm1</td><td>Eurotiomycetes</td><td>Onygenales</td><td></td><td>33</td><td char="." align="char">46.2</td><td>2867</td><td>[<xref ref-type="bibr" rid="CR20">20</xref>]</td></tr><tr><td><italic>Paracoccidioides brasiliensis</italic></td><td>Pb03</td><td>Eurotiomycetes</td><td>Onygenales</td><td></td><td>29</td><td char="." align="char">44.5</td><td>552</td><td>[<xref ref-type="bibr" rid="CR22">22</xref>]</td></tr><tr><td><italic>Trichoderma reesei</italic></td><td>QM6a</td><td>Sordariomycetes</td><td>Hypocreales</td><td></td><td>33</td><td char="." align="char">52.8</td><td>131</td><td>[<xref ref-type="bibr" rid="CR23">23</xref>]</td></tr><tr><td><italic>Neurospora crassa</italic></td><td>OR74A</td><td>Sordariomycetes</td><td>Sordariales</td><td></td><td>41</td><td char="." align="char">48.3</td><td>411</td><td>[<xref ref-type="bibr" rid="CR24">24</xref>]</td></tr><tr><td><italic>Saccharomyces cerevisiae</italic></td><td>S288C</td><td>Saccharomycetes</td><td>Saccharomycetales</td><td></td><td>12</td><td char="." align="char">38.3</td><td>16</td><td>[<xref ref-type="bibr" rid="CR25">25</xref>]</td></tr></tbody></table><table-wrap-foot><p>The novel genomes generated in this study are in bold. The order of species follows the taxonomic organization (Fig. <xref rid="Fig1" ref-type="fig">1a</xref>)</p></table-wrap-foot></table-wrap><fig id="Fig1"><label>Fig. 1</label><caption><p>Genome overview of <italic>Aspergillus</italic> and comparative species. <bold>a</bold> Core genes, based on MCL clustering of protein sequences, and cluster membership in section <italic>Nigri</italic> and the Aspergillaceae. <italic>Pink</italic> area of <italic>pie charts</italic> indicates proteins assignable to one or more Pfam domain; <italic>white</italic> or <italic>gray</italic> areas indicate proteins with no Pfam domain. The majority of proteins conserved in Section Nigri, Aspergillaceae, or the full set of comparative fungi could be assigned to a Pfam. Contrastingly, most clade-specific proteins (occurring only in Section Nigri or Aspergillaceae) were not assignable to any Pfam. <bold>b</bold> Maximum likelihood phylogeny inferred from 149 conserved protein sequences. Organisms newly sequenced for this study are indicated in <italic>bold</italic>. All bootstrap values are 100 except where indicated. Section <italic>Nidulantes</italic> is inferred to be a sister group to section <italic>Nigri</italic>, in contrast to previous studies. Letters in <italic>green</italic> behind the strain numbers indicate the reproductive state: <italic>A</italic> asexual, <italic>S-HO</italic> sexual homothallic, <italic>S-HE</italic> sexual heterothallic. <bold>c</bold> Protein conservation, inferred from MCL clustering of proteins, indicates that the majority of proteins in Aspergillaceae have homologs in other fungi, <italic>bars</italic> showing number of proteins being aligned to individual species to the <italic>left-hand side</italic> in (<bold>b</bold>). Some 21% of proteins are specific to the Aspergillaceae, while 14% of proteins in section <italic>Nigri</italic> are specific to that clade. Organism-specific proteins make up 9% for the Aspergillaceae as a whole and 8% for section <italic>Nigri</italic></p></caption><graphic xlink:href="13059_2017_1151_Fig1_HTML" id="MO1"></graphic></fig></p><p>A substantial proportion (80% on average) of the identified genes in Aspergillaceae genomes have homologs in other lineages of fungi, indicating that around 20% are specific to Aspergillaceae. Many such genes are specific to a clade, e.g. the genomes of section <italic>Nigri</italic> contain an average of ~1800 <italic>Nigri</italic>-specific genes (Fig. <xref rid="Fig1" ref-type="fig">1a</xref>). The number of unique genes per species differs significantly, even between the three <italic>A. niger</italic> genomes included in the analysis (Fig. <xref rid="Fig1" ref-type="fig">1b and c</xref>). However, different approaches to genome annotation and gene calling may have contributed to these differences, given that not all genomes were sequenced at the same time or by the same technology, nor analyzed with the same software. Therefore, the true number of unique genes is likely to be lower. There is also the possibility that some apparent differences are caused by genes missing due to gaps in the different genome sequences. Protein sequence identity within the Aspergillaceae ranges from 64% (e.g. between <italic>A. zonatus</italic> and <italic>A. versicolor</italic>) to 99% in <italic>A. niger</italic> strains NRRL3 and ATCC 1015, which compares to the average 68% amino acid identity reported in previous studies, and is similar to the divergence between mammals and fish [<xref ref-type="bibr" rid="CR3">3</xref>].</p><p>A genome-wide phylogenetic analysis was conducted to determine the relationship between the newly sequenced genomes and other related species present in MycoCosm. This resulted in a highly supported phylogram providing insights into taxonomic relationships within <italic>Aspergillus</italic> and between <italic>Aspergillus</italic> and related genera. With the introduction of the single name nomenclature for fungal anamorph and teleomorph forms, there is discussion over whether to split <italic>Aspergillus</italic> or to maintain the genus as one. One argument for splitting is the indication that the genus is paraphyletic. In previous taxonomic studies on <italic>Aspergillaceae</italic>, up to five genes were studied and deeper nodes in these phylograms were either poorly or not supported [<xref ref-type="bibr" rid="CR26">26</xref>, <xref ref-type="bibr" rid="CR27">27</xref>]. An important finding is that our analysis using 149 conserved protein sequences (Fig. <xref rid="Fig1" ref-type="fig">1b</xref>) places almost all <italic>Aspergillus</italic> species in a monophyletic clade that is sister to a clade containing <italic>Penicillium</italic> species. The only exception was <italic>A. zonatus</italic>, which is consistent with studies suggesting that <italic>A. zonatus</italic> is incorrectly classified in <italic>Aspergillus</italic> and is instead most closely related to <italic>Penicilliopsis clavariiformis</italic> [<xref ref-type="bibr" rid="CR26">26</xref>]. The genus <italic>Aspergillus</italic> has traditionally been classified into a number of subgenera and sections based on morphological and phylogenetic analysis, although precise relationships for many groups have remained uncertain [<xref ref-type="bibr" rid="CR19">19</xref>]. Our analysis indicates that the subgenus <italic>Circumdati</italic> appears to be polyphyletic, with <italic>A. flavus</italic>, <italic>A. oryzae</italic>, and <italic>A. terreus</italic> forming one clade and the black aspergilli (sect. <italic>Nigri</italic>) forming a separate clade. <italic>Aspergillus versicolor</italic>, <italic>A. sydowii</italic>, and <italic>A. nidulans</italic>, all members of the section <italic>Nidulantes</italic>, were positioned between these two clades. <italic>Aspergillus wentii</italic> occupied a basal position in the subgenus <italic>Aspergillus</italic> near to <italic>A. glaucus</italic> and <italic>A. ruber</italic>, consistent with the xerophilic nature of other species in this subgenus. Within the section <italic>Nigri</italic>, <italic>A. luchuensis</italic> (previously referred to as <italic>A. foetidus</italic> or <italic>A. acidus</italic> [<xref ref-type="bibr" rid="CR28">28</xref>]) and <italic>A. tubingensis</italic> were sister species related to <italic>A. niger</italic>, while <italic>A. brasiliensis</italic> occupied a more basal position in agreement with other phylogenetic analyses [<xref ref-type="bibr" rid="CR1">1</xref>, <xref ref-type="bibr" rid="CR29">29</xref>].</p></sec><sec id="Sec4"><title>Asexual and sexual reproduction</title><p>One reason for the widespread occurrence of <italic>Aspergillus</italic> species is their ability to produce prolific numbers of mitotically derived conidia, which are dispersed by wind and colonize new substrates. These asexual spores are produced from conidiophores, which have a characteristic structure in most aspergilli consisting of a stalk with a vesicle bearing phialides from which chains of conidia radiate outwards [<xref ref-type="bibr" rid="CR30">30</xref>, <xref ref-type="bibr" rid="CR31">31</xref>]. About 64% of <italic>Aspergillus</italic> species are known to reproduce only by asexual means, but the remainder can also reproduce sexually, forming structures known as cleistothecia within which meiotically derived ascospores are produced [<xref ref-type="bibr" rid="CR32">32</xref>]. Where sexual reproduction occurs, it involves either homothallic (self-fertility) or heterothallic (obligate out-crossing) breeding systems, with different types of cleistothecia produced according to taxonomic grouping [<xref ref-type="bibr" rid="CR33">33</xref>, <xref ref-type="bibr" rid="CR34">34</xref>]. The diversity of reproductive modes and their associated morphologies in the aspergilli provide excellent opportunities to study the evolutionary genetics of asexual and sexual reproduction in fungi.</p><sec id="Sec5"><title>Asexual reproduction</title><p>The regulation of asexual sporulation (conidiation) has been extensively studied in the model fungus <italic>A. nidulans</italic>. Many regulatory genes have been identified and can be divided into central regulators, upstream activators, negative regulators, light-responsive, and <italic>velvet</italic> regulators (Fig. <xref rid="Fig2" ref-type="fig">2a</xref>) [<xref ref-type="bibr" rid="CR35">35</xref>]. A central regulatory pathway (<italic>brlA</italic>, <italic>abaA</italic>, and <italic>wetA</italic>) controls conidiation-specific gene expression and asexual developmental processes [<xref ref-type="bibr" rid="CR36">36</xref>]. Proper activation of <italic>brlA</italic> requires upstream developmental activators (encoded by <italic>fluG</italic>, <italic>flbA</italic>-<italic>E</italic>) [<xref ref-type="bibr" rid="CR30">30</xref>] and removal of repression by several negative regulators (including SfgA, VosA, NsdD, and two G-protein signaling pathways; see “<xref rid="Sec33" ref-type="sec">Signal transduction pathway</xref>” section below) [<xref ref-type="bibr" rid="CR35">35</xref>, <xref ref-type="bibr" rid="CR37">37</xref>]. Light also regulates expression of asexual developmental genes, including <italic>brlA</italic> and upstream activators, with several photoreceptors identified such as one red-light (FphA) and three blue-light receptors [<xref ref-type="bibr" rid="CR38">38</xref>]. Moreover, <italic>velvet</italic> regulators can interact with each other and with non-<italic>velvet</italic> proteins to control development and sporogenesis [<xref ref-type="bibr" rid="CR39">39</xref>]. Comparison of the conidiation system of <italic>A. nidulans</italic> to other aspergilli revealed that the regulatory genes are highly conserved, suggesting similar triggers and signaling of the conidiation regulatory pathways in this genus (Additional file <xref rid="MOESM2" ref-type="media">2</xref>). The central regulatory pathway (<italic>brlA</italic> → <italic>abaA</italic> → <italic>wetA</italic>) is present in all <italic>Aspergillus</italic> and <italic>Penicillium</italic> genomes, whereas only one or two elements of this pathway were found in the Ascomycotina in general, so making this a central conserved feature of the aspergilli and penicillia (Fig. <xref rid="Fig2" ref-type="fig">2b</xref>). Normally, these and other regulatory genes were only present in single copy. However, some absences and occurrences of gene duplication were observed (Additional file <xref rid="MOESM2" ref-type="media">2</xref>). Notably, <italic>Monascus ruber</italic> lacks an <italic>abaA</italic> homolog, correlating with a change in conidiation form [<xref ref-type="bibr" rid="CR40">40</xref>], whereas <italic>A. oryzae</italic> and <italic>A. carbonarius</italic> have two copies of <italic>abaA</italic> and <italic>wetA</italic>. Regarding upstream developmental activators, almost half of the species, including <italic>A. flavus</italic>, <italic>A. fumigatus</italic>, and <italic>A. terreus</italic>, possess two copies of the <italic>fluG</italic> gene, suggesting more differentiated regulation of development in these species. Two copies of the blue light responsive <italic>lreA</italic> and <italic>lreB</italic> transcription factor genes were found in <italic>A. carbonarius</italic> and related experimental work showed this species had the highest levels of asexual sporulation in blue light (relative to white light) of all tested aspergilli (Additional files <xref rid="MOESM2" ref-type="media">2</xref> and <xref rid="MOESM3" ref-type="media">3</xref>). Finally, multiple copies of the <italic>fphA</italic> red light receptor were found in some species, although in this case there was no clear correlation with the extent of asexual sporulation under different light treatments (Additional file <xref rid="MOESM4" ref-type="media">4</xref>).<fig id="Fig2"><label>Fig. 2</label><caption><p>Regulatory pathway of asexual sporulation in <italic>A. nidulans</italic>. <bold>a</bold> Central regulators, upstream activators, negative regulators, velvet regulators, and light-responsive regulators are illustrated by <italic>green</italic>, <italic>light purple</italic>, <italic>blue</italic>, <italic>dark purple</italic>, and <italic>red icons</italic>, respectively. <bold>b</bold> Distribution of central regulators for asexual sporulation in 85 fungi. These fungi are representatives from the phyla Ascomycota, Basidiomycota, Chytridiomycota, and Zygomycota. Their genome protein sequences were searched for homologs of AbaA, BrlA, and WetA by BlastP using sequences of <italic>A. nidulans</italic> AbaA, BrlA, and WetA as queries. Details of these fungi are presented in Central Regulator Strain Information. As shown, BrlA seems to be limited to the Eurotiales group, suggesting a specific role for conidiation in Eurotiales fungi. By contrast, WetA is widely distributed in Pezizomycotina fungi, which suggests a general function for the synthesis of cell wall layers to make conidia mature and impermeable. Surprisingly, AbaA is widespread being found in the phyla Ascomycota, Basidiomycota, and Zygomycota, suggesting that AbaA is involved not only in conidial development, but also has other general functions in fungal development</p></caption><graphic xlink:href="13059_2017_1151_Fig2_HTML" id="MO2"></graphic></fig></p></sec><sec id="Sec6"><title>Sexual reproduction</title><p>The apparently asexual nature of the majority of <italic>Aspergillus</italic> species has precluded the use of the sexual cycle as a tool for strain improvement and genetic analysis in them. However, there is accumulating evidence that many such supposedly asexual species have the potential for sexual reproduction if the correct mating partners and environmental conditions to induce sexuality can be identified [<xref ref-type="bibr" rid="CR32">32</xref>, <xref ref-type="bibr" rid="CR33">33</xref>]. The <italic>Aspergillus</italic> species included in this study were typical in that the majority of them have no known sexual cycle (Additional file <xref rid="MOESM5" ref-type="media">5</xref>). To investigate whether the asexual species may have a cryptic sexual cycle, the presence and expression of both mating-type (<italic>MAT</italic>) genes conferring sexual identity [<xref ref-type="bibr" rid="CR41">41</xref>] and a pheromone signaling pathway involved with mating [<xref ref-type="bibr" rid="CR42">42</xref>] were explored. All of the presumed asexual species were found to contain either a <italic>MAT1-1</italic> alpha gene or <italic>MAT1-2</italic> gene encoding a high-mobility group domain protein, with adjacent gene synteny conserved across all species. This is consistent with heterothallism, involving the presence of either <italic>MAT1-1</italic> or <italic>MAT1-2</italic> idiomorphs [<xref ref-type="bibr" rid="CR41">41</xref>]. All of the presumed asexual species also contain <italic>ppgA</italic> homologs encoding a pheromone precursor, and <italic>preA</italic> and <italic>preB</italic> homologs encoding pheromone receptors (Additional file <xref rid="MOESM5" ref-type="media">5</xref>). These species were grown under conditions conducive to sexual reproduction in the aspergilli and gene expression was monitored by reverse transcriptase polymerase chain reaction (RT)-PCR. It was found that the <italic>MAT1-1</italic> or <italic>MAT1-2</italic>, <italic>ppgA</italic>, <italic>preA</italic>, and <italic>preB</italic> genes were expressed in all of the asexual species in the same way as known sexual species, as shown by the detection of spliced transcripts (although exact expression levels were not determined) (Additional file <xref rid="MOESM6" ref-type="media">6</xref>). This suggests that key genes for sexual reproduction may be active in the asexual species. These results are of importance as they suggest the possibility of inducing the sexual cycle in species of biotechnological importance such as <italic>A. niger</italic>, as has recently been achieved for the penicillin producer <italic>P. chrysogenum</italic> [<xref ref-type="bibr" rid="CR43">43</xref>]. This could accelerate cell-engineering efforts, because sexual crosses would become possible. These results also bring into question the supposed predominance of asexuality in the aspergilli. However, it has to be considered that at least 75 other genes are required for completion of the sexual cycle in the aspergilli [<xref ref-type="bibr" rid="CR33">33</xref>]. Mutation or lack of expression in any of these genes may be responsible for asexuality if fixed within populations, although previous genome studies found no evidence for gene loss or mutation in over 200 genes implicated in fungal mating in <italic>A. oryzae</italic> and <italic>A. niger</italic> [<xref ref-type="bibr" rid="CR4">4</xref>, <xref ref-type="bibr" rid="CR10">10</xref>].</p><p>One other outstanding question concerning the evolution of sex in <italic>Aspergillus</italic> species is whether the ancestral state was homothallism or heterothallism. It has been argued that homothallic fungi are derived from heterothallic ancestors [<xref ref-type="bibr" rid="CR44">44</xref>]. However, given the predominance of homothallic species among the aspergilli and initial analysis of <italic>MAT</italic> gene organization, it has been suggested that homothallism was ancestral in the aspergilli with subsequent conversion to heterothallism [<xref ref-type="bibr" rid="CR4">4</xref>, <xref ref-type="bibr" rid="CR45">45</xref>]. One key piece of supporting evidence was that heterothallism was presumed to be rare in the aspergilli. However, our findings indicate that many supposedly asexual <italic>Aspergillus</italic> species are in fact heterothallic in nature, and this is true across the wide taxonomic diversity of aspergilli under study (Fig. <xref rid="Fig1" ref-type="fig">1b</xref>). This indicates that heterothallism is widespread in the aspergilli, with a conserved organization and synteny of the mating-type (<italic>MAT</italic>) locus observed in the current study. This also contrasts with the variation in organization of <italic>MAT</italic> loci observed in homothallic <italic>Aspergillus</italic> species [<xref ref-type="bibr" rid="CR4">4</xref>, <xref ref-type="bibr" rid="CR46">46</xref>–<xref ref-type="bibr" rid="CR48">48</xref>]. Overall, our results strongly support the hypothesis that the aspergilli are evolved from a heterothallic ancestor, with homothallic species arising due to divergent forms of <italic>MAT</italic> gene arrangement as previously reported for <italic>Cochliobolus</italic> species [<xref ref-type="bibr" rid="CR44">44</xref>]. This conclusion is of significance for future attempts to induce sexual reproduction in asexual species and possible genetic manipulation of <italic>MAT</italic> genes to induce sexuality [<xref ref-type="bibr" rid="CR41">41</xref>].</p></sec></sec><sec id="Sec7"><title>Primary carbon metabolism</title><p>Fungi are well-known for their ability to exploit a wide range of simple and complex carbon substrates for growth [<xref ref-type="bibr" rid="CR49">49</xref>, <xref ref-type="bibr" rid="CR50">50</xref>]. Differences in their primary metabolism may partly help to explain the diversity of fungal phenotypes. We experimentally and genetically analyzed three traits of fungal primary metabolism in the aspergilli to examine possible links to genome diversity, namely carbon source utilization, presence of alternative oxidases, and organic acid production.</p><sec id="Sec8"><title>Carbon source utilization</title><p>The genomes of 19 aspergilli were analyzed for copy numbers of carbon catabolic genes and compared for growth on 11 different monomeric and dimeric carbon sources (Fig. <xref rid="Fig3" ref-type="fig">3a</xref>, Additional files <xref rid="MOESM6" ref-type="media">6</xref> and <xref rid="MOESM7" ref-type="media">7</xref>). A nearly complete correlation was found between the presence of genes predicted to encode catabolic enzymes and the ability to grow on a specific carbon source. Exceptions to this were the inability of <italic>A. niger</italic> to grow on D-galactose and lactose, but it is known that the relevant transport and germination triggers for these carbon sources are not active in <italic>A. niger</italic> spores [<xref ref-type="bibr" rid="CR51">51</xref>–<xref ref-type="bibr" rid="CR53">53</xref>] (Fig. <xref rid="Fig3" ref-type="fig">3a</xref>). Furthermore, <italic>A. clavatus</italic> and <italic>A. zonatus</italic> can grow on sucrose despite having no apparent invertases in their genomes. This could be due to genes missing in the assembly, the activity of α-glucosidases [<xref ref-type="bibr" rid="CR54">54</xref>], non-specific enzymes, or a so far unknown type of invertase possibly found outside the standard GH32 Carbohydrate Active enZyme (CAZy) invertase family.<fig id="Fig3"><label>Fig. 3</label><caption><p>Experimental and in silico analysis of central metabolism. Clustering of the species was performed based on <italic>gpdA</italic> and orthologs from all genomes. <bold>a</bold> Catabolism of 11 sugars correlated to the number of isoenzymes investigated for each of the 11 catabolic pathways. A cross line marks all conditions where not growth was observed. <bold>b</bold> Copy numbers of (putative) alternative oxidases (<italic>aox</italic>) compared to growth assays on plates with agents inhibiting either the standard oxidative phosphorylation (KCN) or Aox (SHAM). <bold>c</bold> Correlation of putative isoenzymes for activities involved in organic acid formation and produced organic acids</p></caption><graphic xlink:href="13059_2017_1151_Fig3_HTML" id="MO3"></graphic></fig></p><p>In general, extra copies of a catabolic pathway, or steps thereof, did not confer more efficient carbon utilization under the conditions tested, possibly due to differential expression or altered substrate specificity of the paralogs. It was further observed that gene copy number of specific enzymes was generally correlated with phylogenetic relationships, in contrast to the increased levels of genetic diversity and horizontal gene transfer observed for secondary metabolism among closely related species (see below).</p></sec><sec id="Sec9"><title>Alternative oxidase</title><p>A characteristic feature of fungal mitochondria is the presence of an additional terminal oxidase, the alternative oxidase (Aox), alongside the cytochrome-dependent one. Aox catalyzes the reduction of oxygen to water, bypassing respiratory complexes III and IV of the cytochrome-mediated electron transport chain. All examined species showed the presence of at least one alternative oxidase (<italic>aox</italic>) gene (Fig. <xref rid="Fig3" ref-type="fig">3b</xref>). Growth experiments confirmed that all <italic>Aspergillus</italic> species grew well in the presence of potassium cyanide (KCN), which inhibits the cytochrome pathway (Additional file <xref rid="MOESM8" ref-type="media">8</xref>). Addition of salicylhydroxamic acid (SHAM), which inhibits Aox, as well as KCN stunted or eliminated growth of nearly all species except <italic>A. niger</italic> and <italic>A. aculeatus</italic>. In general, the section <italic>Nigri</italic> exhibited higher tolerance to SHAM and KCN and grew faster than other aspergilli. As with the primary metabolism above, this increased growth could not be explained by changes in gene copy numbers as the <italic>Nigri</italic> had similar or lower <italic>aox</italic> copy numbers than other species (Fig. <xref rid="Fig3" ref-type="fig">3b</xref>).</p></sec><sec id="Sec10"><title>Organic acid production</title><p>Organic acid production by <italic>A. niger</italic> is a process of major industrial importance. We examined the number of putative isoenzymes associated with citric acid and gluconic acid production in each of the 19 genomes and measured the concentration of relevant organic acids produced on three different growth media (Fig. <xref rid="Fig3" ref-type="fig">3c</xref>, Additional file <xref rid="MOESM9" ref-type="media">9</xref>). This revealed a close link between the number of isoenzymes and phylogeny, most markedly for the section <italic>Nigri</italic>, in which a series of extra isoenzymes relevant to citrate and gluconic acid production was found, correlating with increased acid production (Additional files <xref rid="MOESM9" ref-type="media">9</xref>A and B). This is in accord with this group being prolific producers of these two organic acids and suggests the evolution of specialized enzymes for this purpose. Indeed, transcriptome analysis of <italic>A. niger</italic>, <italic>A. oryzae</italic>, <italic>A. fumigatus</italic>, and <italic>A. nidulans</italic> showed that orthologs of citrate synthase, pyruvate dehydrogenase, isocitrate dehydrogenase, and malate dehydrogenase were highly expressed in <italic>A. niger</italic> relative to the other species (Additional file <xref rid="MOESM10" ref-type="media">10</xref>C), consistent with metabolic specialization.</p></sec></sec><sec id="Sec11"><title>Plant biomass degradation</title><sec id="Sec12"><title>Genomic comparison</title><p>Several aspergilli have a long history of use as producers of plant polysaccharide modifying and degrading enzymes [<xref ref-type="bibr" rid="CR55">55</xref>, <xref ref-type="bibr" rid="CR56">56</xref>]. Their broad ability to degrade these substrates helps to explain their presence in many different habitats, employing what has been considered a generalist lifestyle with respect to carbon utilization. This means that they do not specialize in any particular plant component, but have the ability to degrade all plant biomass polysaccharides [<xref ref-type="bibr" rid="CR57">57</xref>, <xref ref-type="bibr" rid="CR58">58</xref>]. However, this has so far only been investigated for a relatively small number of species. Therefore, in this study we evaluated plant biomass degrading ability across a larger set of <italic>Aspergillus</italic> species and compared this ability to other ascomycete fungi. Comparison of the number of genes per CAZy family involved in plant biomass degradation revealed strong differences among the species investigated (Table <xref rid="Tab2" ref-type="table">2</xref>, Additional file <xref rid="MOESM10" ref-type="media">10</xref>), although species from the same section generally contained similar numbers of genes. This comparison was based on the family (and subfamily where possible) designations set by the CAZy database (<ext-link ext-link-type="uri" xlink:href="http://www.cazy.org/">www.cazy.org</ext-link>) [<xref ref-type="bibr" rid="CR59">59</xref>]. Exceptions to this were, for example, the lower number of (hemi-) cellulases for <italic>A. carbonarius</italic> compared to other species of the section <italic>Nigri</italic> and that <italic>A. versicolor</italic> is particularly enriched in inulinases compared to other species of the section <italic>Nidulantes</italic> (Table <xref rid="Tab2" ref-type="table">2</xref>). Interestingly, the two most established enzyme producers of this genus, <italic>A. niger</italic> and <italic>A. oryzae</italic>, do not contain the highest number of genes required for degradation of any of the polysaccharides, with the exception of pectin for which the highest number was found in the <italic>A. oryzae</italic> genome (Table <xref rid="Tab2" ref-type="table">2</xref>). The itaconic acid producer <italic>A. terreus</italic> has the highest number of putative cellulases and xyloglucanases, while <italic>A. versicolor</italic> and <italic>A. nidulans</italic> contain the highest numbers of putative xylanases and mannanases, respectively. Gene numbers related to the degradation of the storage polysaccharides starch and inulin are, in general, higher in the sister genera of <italic>Aspergillus</italic> (e.g. <italic>Penicillium</italic>).<table-wrap id="Tab2"><label>Table 2</label><caption><p>Gene numbers related to degradation of different plant-based polysaccharides detected in genomes of selected ascomycete fungi</p></caption><graphic xlink:href="13059_2017_1151_Tab2_HTML" id="MO4"></graphic><table-wrap-foot><p>Only families that can be assigned to a specific polysaccharide, based on currently available data, are included. Highest numbers for any of the polysaccharides are highlighted in green</p></table-wrap-foot></table-wrap></p><p>When comparing specific enzymes, highly variable gene numbers were observed for GH5_7 and GH26 endomannanases, GH32 endoinulinases, GH28 endorhamnogalacturonases, GH43 α-L-arabinofuranosidases, and GH115 α-glucuronidases (Additional file <xref rid="MOESM11" ref-type="media">11</xref>). Only some species contain genes encoding CE15 glucuronoyl esterases, GH45 endoglucanases, and PL11 rhamnogalacturonan lyases. While most of the feruloyl esterase encoding genes are included in the CAZy database, comparison of genes encoding these enzymes also revealed high variability, confirming the considerable diversity in feruloyl esterase activities recently reported for a smaller set of aspergilli [<xref ref-type="bibr" rid="CR60">60</xref>]. This diversity is in part due to the absence of specific orthologs in some species, resulting in differences in the overall gene set per species (Additional file <xref rid="MOESM11" ref-type="media">11</xref>).</p><p>High variability was also observed in the number of genes encoding oxidative enzymes in the genomes analyzed (Additional file <xref rid="MOESM10" ref-type="media">10</xref>), which can also be involved in plant biomass degradation. Numbers in families AA1 (containing laccase), AA3_1 (cellobiose dehydrogenase), AA7 (containing vanillyl alcohol oxidase), and AA9 (lytic polysaccharide monooxygenases) are in the ranges of 5–18, 1–4, 0–7, and 3–12, respectively, but in general the variation within each section is relatively low.</p></sec><sec id="Sec13"><title>Correlation of gene content to growth and enzyme production</title><p>To assess any correlation between CAZy gene content and growth, strain profiling was performed by determining growth on 33 carbon sources which contained plant-related monosaccharides, oligosaccharaides, and polysaccharides as well as crude plant-based substrates, and no-carbon source and casein as controls (Additional file <xref rid="MOESM8" ref-type="media">8</xref>). Full profiles can be found at [<xref ref-type="bibr" rid="CR61">61</xref>]. A hierarchical clustering (HCL) correlation analysis was performed on the number of genes per CAZy family for the tested species. Figure <xref rid="Fig4" ref-type="fig">4a</xref> shows that overall the evolution of CAZy families is similar to the taxonomic relationship of the species (compare to Fig. <xref rid="Fig1" ref-type="fig">1a</xref>). In this analysis, families that become more or less abundant simultaneously group together. No clear overall clustering of CAZy families related to the same substrate could be observed. This is likely due to the presence of multiple polymers in any plant biomass, requiring the production of enzymes acting on different substrates. In addition, commercial substrates used are unlikely to be identical to those encountered in nature and may therefore limit the observed specificity. In some cases, two to three enzyme families related to the same substrate did cluster, such as GH88/GH78/PL1 and PL3/PL9 (pectin), GH7/AA9 (cellulose), and GH27/GH36 and GH5_7/GH134 (galactomannan). In contrast, when the ability of these fungi to grow on polysaccharides (Additional file <xref rid="MOESM8" ref-type="media">8</xref>) was quantified and used for HCL, the taxonomic organization was largely lost (Fig. <xref rid="Fig4" ref-type="fig">4b</xref>). This suggests that despite conserved CAZome evolution, the ability of an individual species to degrade a specific substrate is dependent on other factors such as the regulation of gene expression or the transport of monomers. Therefore, as observed recently for eight aspergilli [<xref ref-type="bibr" rid="CR57">57</xref>], no clear correlation between CAZome, taxonomy, and enzyme sets produced on plant biomass substrates could be detected. A possible explanation for this is that under laboratory conditions only complete disappearance of a CAZy family would result in loss of function. However, the persistence of the CAZy genes clearly indicates an evolutionary pressure to maintain them in the genomes, which could be due to the more complex natural environment. A better understanding of fungal biotopes, including the actual components of the available substrates they consume in nature, will likely reveal a better correlation between genome content and carbohydrate preference of each species.<fig id="Fig4"><label>Fig. 4</label><caption><p>HCL (<bold>a</bold>) the number of genes per CAZy family related to plant biomass degradation in the tested genomes and (<bold>b</bold>) the relative growth of the tested species on polymeric substrates. <italic>Color coding</italic> in (<bold>a</bold>) refers to the polysaccharide these families act on. Black families either contain multiple activities or are active on multiple polysaccharides. For the other colors: <italic>pink</italic> = guar gum (galactomannan), <italic>purple</italic> = starch, <italic>red</italic> = xylan, <italic>green</italic> = pectin, <italic>orange</italic> = inulin, <italic>dark blue</italic> = cellulose, <italic>pale blue</italic> = xyloglucan</p></caption><graphic xlink:href="13059_2017_1151_Fig4_HTML" id="MO5"></graphic></fig></p><p>To assess the impact on growth arising from differences in the number of genes encoding oxidative enzymes, 20 aspergilli were grown in minimal medium (MM) with 1% cotton seed hulls over 14 days and were assayed for laccase and cellobiose dehydrogenase activities (Additional file <xref rid="MOESM12" ref-type="media">12</xref>). The highest laccase activity was observed for <italic>A. fischeri</italic> and low activities were detected for <italic>A. oryzae</italic>, <italic>A. wentii</italic>, and <italic>A. versicolor</italic>. No laccase activity could be detected for 11 of the aspergilli. The highest cellobiose dehydrogenase levels were measured for <italic>A. fumigatus</italic>, <italic>A. wentii</italic>, <italic>A. tubingensis</italic>, and <italic>A. terreus</italic>. No cellobiose dehydrogenase activity was detected for five aspergilli. Thus, there was no clear correlation between these observed enzyme activities and the number of genes in the respective genomes (Additional file <xref rid="MOESM10" ref-type="media">10</xref>).</p><p>Recently, Benoit et al. compared the production of plant biomass degrading enzymes by eight aspergilli during growth on wheat bran or sugar beet pulp [<xref ref-type="bibr" rid="CR57">57</xref>]. This work was extended in the present study to include the newly sequenced species, using the same culture conditions and data analysis as in the previous study. These substrates provide useful comparative datasets because both contain cellulose, but differ in that wheat bran is rich in xylan, while sugar beet pulp contains large amounts of pectin and xyloglucan. The results demonstrated a large variation in enzyme production between the aspergilli, even for species within the same section (Fig. <xref rid="Fig5" ref-type="fig">5</xref>). Most species produced predominantly cellulose-active and xylan-active enzymes during growth on wheat bran, but the ratio between these two enzyme groups varied strongly in some species (Fig. <xref rid="Fig5" ref-type="fig">5a</xref>). Some unusual profiles were also observed, such as the high relative amount of different pectinases produced by <italic>A. fischeri</italic>, the low amount of xylanases for <italic>A. carbonarius</italic>, and the high amount of amylases for <italic>A. oryzae</italic>. On sugar beet pulp, nearly all species produced high amounts of pectinases, appropriate to the composition of the substrate (Fig. <xref rid="Fig5" ref-type="fig">5b</xref>). An exception to this was <italic>A. clavatus</italic>, where genome analysis had already revealed a strong reduction in genes encoding pectin-active enzymes [<xref ref-type="bibr" rid="CR57">57</xref>]. <italic>A. clavatus</italic> compensates by high production of cellulases, whereas cellulases are almost absent in the profiles of several other species (e.g. <italic>A. wentii</italic>, <italic>A. fischeri</italic>, <italic>A. flavus</italic>, <italic>A. tubingensis</italic>). The high production of xylanases by <italic>A. aculeatus</italic> and to a lesser extent by <italic>A. luchuensis</italic> was also unexpected.<fig id="Fig5"><label>Fig. 5</label><caption><p>Comparative proteomics of aspergilli during growth on wheat bran (<bold>a</bold>) and sugar beet pulp (<bold>b</bold>). Results are summarized by the polysaccharide that the enzymes act upon. Only CAZy families specific for one polysaccharide are included in the comparison. Cellulose-active enzymes: GH6, GH7, GH12, GH45, GH74, AA9; xylan-active enzymes: CE1, CE15, GH10, GH11, GH62, GH67, GH115; pectin-active enzymes: CE8, CE12, GH28, GH35, GH51, GH53, GH54, GH78, GH88, GH93, GH105, PL1, PL3, PL4, PL9, PL11; starch-active enzymes: GH13, GH15; other (CAZy families with multiple activities or minor activities on the substrates): CE16, GH1, GH2, GH3, GH5, GH26, GH27, GH31, GH32, GH36, GH43, GH95. Extracellular proteins following trypsin digestion were analyzed by LC-MS/MS using a LTQ-Orbitrap Velos mass analyzer (Thermo-Fisher). Quantification was based on MS precursor ion signal. Extracted ion chromatograms were used to determine the peptide area value associated to each identified precursor ion. A protein area value was calculated as the average of the three most intense, distinct peptides assigned to a protein. The amounts of proteins associated with each enzyme activity were expressed as percentage of the amount of total extracellular proteins present in each culture condition</p></caption><graphic xlink:href="13059_2017_1151_Fig5_HTML" id="MO6"></graphic></fig></p><p>The variation in detected enzymes in the proteomic data of the species investigated here far exceeded that which could be explained by genome variation, consistent with previous results from the first eight <italic>Aspergillus</italic> species to be genome sequenced [<xref ref-type="bibr" rid="CR57">57</xref>]. This suggests that the observed variation is mainly caused by regulatory changes, rather than simply by gene copy number. Since all species contain the same set of conserved regulators for cellulase, xylan, and pectin degradation (data not shown), they presumably have a different fine-tuning of the regulatory system. This could be due to a different range of target genes for their regulators or different functioning of them, as was recently demonstrated for the major (hemi-) cellulolytic regulator XlnR [<xref ref-type="bibr" rid="CR62">62</xref>]. The exoproteome analysis reported here confirms our recent observation [<xref ref-type="bibr" rid="CR57">57</xref>] that the enzyme cocktails produced by these fungi in response to the same plant biomass are highly different and will therefore also have different efficiencies in saccharification of plant-derived biomass.</p></sec></sec><sec id="Sec14"><title>Secondary metabolism</title><p>The ability to produce secondary metabolites (SM) is an important feature of many fungi and certainly of the aspergilli and related fungi. These metabolites are involved in many processes in nature, such as communication between fungi and competition for nutrients and can be pathogenicity factors. Some of these metabolites have become widely used as antibiotics. In this section, we highlight the diversity of SM production in the aspergilli and the role of cytochrome P450 (CYP) genes in secondary metabolism.</p><sec id="Sec15"><title>Secondary metabolite biosynthesis gene clusters in the aspergilli</title><p>Polyketide synthases (PKSs), non-ribosomal peptide synthetases (NRPSs), or dimethylallyl tryptophan transferases (DMATs) are involved in the biosynthesis of the vast majority of SM products [<xref ref-type="bibr" rid="CR63">63</xref>, <xref ref-type="bibr" rid="CR64">64</xref>]. The PKS and NRPS genes are frequently clustered together with other pathway genes, such as DMAT genes, involved with processing of the initial product to form the final SM, thereby forming a linked gene cluster. The high degree of conservation of these proteins and their specific domain structure allow reliable in silico prediction of their genes. Thus, the <italic>Aspergillus</italic> genomes were searched to gain insights into their evolution and potential to produce SMs. The number of individual PKS, NRPS, and DMAT genes was found to vary considerably from 21 in <italic>A. glaucus</italic> to 66 in <italic>A. tubingensis</italic> and <italic>A. versicolor</italic> (Table <xref rid="Tab3" ref-type="table">3</xref>). These large variations do not correlate with genome size, suggestsing that the number of SM genes and their associated clusters depends on the lifestyle and the corresponding requirements of each species.<table-wrap id="Tab3"><label>Table 3</label><caption><p>Number of predicted SM biosynthesis genes and number of associated clusters in the genomes</p></caption><graphic xlink:href="13059_2017_1151_Tab3_HTML" id="MO7"></graphic><table-wrap-foot><p><italic>Aspergillus</italic> species were ordered according to their phylogenetic relationships (see Fig. <xref rid="Fig1" ref-type="fig">1</xref>)</p></table-wrap-foot></table-wrap></p><p>To date about 50 non-redundant SM gene clusters have been experimentally characterized in the aspergilli. We scanned the 19 genomes for regions syntenic with these known clusters to examine their distribution and thereby determine the potential of the various species for production of SMs. Thirty-six clusters appeared to be conserved with respect to gene content and order, with 23 clusters conserved in more than one genome (Table <xref rid="Tab4" ref-type="table">4</xref>). By contrast, 12 clusters showed no conservation of gene content and order (Table <xref rid="Tab4" ref-type="table">4</xref>). Interestingly, in total, we defined 44 unique PKS, NRPS, or DMAT genes that have no orthologs across all the analyzed 19 species.<table-wrap id="Tab4"><label>Table 4</label><caption><p>Conservation of experimentally characterized clusters in the 18 <italic>Aspergillus</italic> species</p></caption><graphic xlink:href="13059_2017_1151_Tab4_HTML" id="MO8"></graphic><table-wrap-foot><p>The species are ordered according to their phylogenetic relationships. The level of synteny (percentage of syntenic cluster genes) is reflected by the color legend. Clusters are based on previous studies [<xref ref-type="bibr" rid="CR65">65</xref>–<xref ref-type="bibr" rid="CR113">113</xref>]</p></table-wrap-foot></table-wrap></p><p>The degree of similarity between clusters from different species can provide an indication of potential similarities in the products that they synthesize, with clusters having very high similarity (90–100%) normally coding for the same SM. Genome data from the present study therefore allowed us to predict the production of certain SMs. This can be exemplified for the production of pseurotin and penicillin. Pseurotin was previously described for <italic>A. fumigatus</italic> [<xref ref-type="bibr" rid="CR64">64</xref>, <xref ref-type="bibr" rid="CR91">91</xref>–<xref ref-type="bibr" rid="CR93">93</xref>], <italic>A. clavatus</italic> [<xref ref-type="bibr" rid="CR114">114</xref>, <xref ref-type="bibr" rid="CR115">115</xref>], <italic>A. oryzae</italic> [<xref ref-type="bibr" rid="CR116">116</xref>], <italic>A. leporis</italic>, and <italic>A. nomius</italic> [<xref ref-type="bibr" rid="CR117">117</xref>] but so far not for other <italic>Aspergillus</italic> species. The gene cluster in <italic>A. fumigatus</italic> was already known, but here we identified the conserved pseurotin gene cluster in the <italic>A. clavatus</italic> genome. There was no indication of a pseurotin gene cluster in <italic>A. oryzae</italic>, although its production was reported for this species. However, the particular strain reported to produce pseurotin is not available and may have been misidentified. In another example, analysis of the penicillin gene cluster known to be present in <italic>A. nidulans</italic> [<xref ref-type="bibr" rid="CR75">75</xref>], <italic>A. oryzae</italic> [<xref ref-type="bibr" rid="CR118">118</xref>], and <italic>A. flavus</italic> revealed a single additional species, <italic>A. sydowii</italic>, where this cluster is well conserved indicating the potential for penicillin production (Fig. <xref rid="Fig6" ref-type="fig">6</xref>).<fig id="Fig6"><label>Fig. 6</label><caption><p>Conservation of penicillin (<bold>a</bold>) and pseurotin (<bold>b</bold>) biosynthesis gene clusters in <italic>Aspergillus</italic> species</p></caption><graphic xlink:href="13059_2017_1151_Fig6_HTML" id="MO9"></graphic></fig></p><p>In addition, we found examples of clusters with partially conserved synteny (50–90%; Table <xref rid="Tab4" ref-type="table">4</xref>). The SM products of such clusters can be expected to be similar but not identical. For instance, fumiquinazolins were observed in <italic>A. fumigatus</italic> [<xref ref-type="bibr" rid="CR119">119</xref>], whereas in <italic>A. versicolor</italic> and <italic>A. clavatus</italic> there are cottoquinazolins [<xref ref-type="bibr" rid="CR120">120</xref>] and tryptoquivalins [<xref ref-type="bibr" rid="CR121">121</xref>], respectively, which is in agreement with the partial conservation and synteny of the corresponding clusters (Table <xref rid="Tab4" ref-type="table">4</xref>). Similarly, geodin produced by <italic>A. terreus</italic> is related to sulochrins produced by <italic>A. fumigatus</italic> (3-O-methylsulochrin) and <italic>A. wentii</italic> (sulochrin and isosulochrin), consistent with moderate conservation of the respective gene clusters (Table <xref rid="Tab4" ref-type="table">4</xref>).</p><p>In <italic>A. nidulans</italic>, three gene clusters (AN6784, AN9226, and AN11194) are responsible for the biosynthesis of xanthone (shamixanthone and epishamixanthone) and variecoxanthone. It was observed that the shamixanthone cluster (AN6784) is reasonably conserved, with five of nine <italic>A. nidulans</italic> cluster genes being syntenic in <italic>A. sydowii</italic> and <italic>A. versicolor</italic> (Table <xref rid="Tab4" ref-type="table">4</xref>). However, the genes for the other clusters are unique to <italic>A. nidulans</italic>, which is known to produce a much more varied profile of these compounds than <italic>A. sydowii</italic> and <italic>A. versicolor</italic>. Meanwhile, the lack of production of particular SMs by some strains and/or isolates was often confirmed by the genome data. <italic>Aspergillus versicolor</italic> and <italic>A. nidulans</italic> produce sterigmatocystin [<xref ref-type="bibr" rid="CR122">122</xref>], whereas the closely related <italic>A. sydowii</italic> CBS 593.65 does not. This can now be explained by the complete lack of the corresponding gene cluster in <italic>A. sydowii</italic>, whereas the sterigmatocystin cluster is perfectly conserved between <italic>A. versicolor</italic> and <italic>A. nidulans</italic> (Table <xref rid="Tab4" ref-type="table">4</xref>)<italic>.</italic> Thus, our bioinformatic analysis overall supports and provides a genetic basis for previous experimental data.</p><p>Analysis of the genome data also allowed us to predict gene clusters that might be responsible for the biosynthesis of experimentally detected SMs for which the genetic basis had previously been unknown. For example, the three black <italic>Aspergillus</italic> strains, <italic>A. brasiliensis</italic> CBS101740, <italic>A. luchuensis</italic> CBS106.47, and <italic>A. tubingensis</italic> CBS134.48, all produce naptho-gamma-pyrones (Table <xref rid="Tab4" ref-type="table">4</xref>) [<xref ref-type="bibr" rid="CR123">123</xref>]. The gene cluster for the related neosartoricin/fumicycline of <italic>A. fumigatus</italic> and <italic>A. fischeri</italic> has previously been characterized and may be analogous to the naptho-gamma-pyrone cluster in species of the section <italic>Nigri</italic>, given that both gene clusters occur in the same conserved syntenic region across all these species.</p><p>Finally, the analysis led to the discovery of previously unknown, but well conserved, clusters such as that with an AN3386 backbone (Table <xref rid="Tab4" ref-type="table">4</xref>), providing exciting leads for future cluster analysis.</p></sec><sec id="Sec16"><title>CYPomes and supporting cytochrome P450 reductases</title><p>CYP genes are also of interest for secondary metabolism. More than 2300 CYP sequences (PF00067) were identified in the 19 aspergilli examined (data not shown). These numbers are comparable with analysis of the CYPome for <italic>A. nidulans</italic> in the previous CADRE genome annotation [<xref ref-type="bibr" rid="CR124">124</xref>]. Some of the CYP families were further analyzed in the present study relating to their possible use as antifungals and roles in fungal secondary metabolism, namely: CYP51 (sterol 14α-demethylase) [<xref ref-type="bibr" rid="CR125">125</xref>], CYP61 (22-sterol desaturase) [<xref ref-type="bibr" rid="CR126">126</xref>], CYP56 (dityrosine synthesis) [<xref ref-type="bibr" rid="CR127">127</xref>], CYP53 (benzoate 4-hydroxylase) [<xref ref-type="bibr" rid="CR128">128</xref>], CYP630 (oleic acid ω-hydroxylase) [<xref ref-type="bibr" rid="CR129">129</xref>], Ppo (fatty acid oxygenases or oxylipin generating dioxygenases) [<xref ref-type="bibr" rid="CR130">130</xref>], and a supporting enzyme CYP reductase (CPR) as well as CYP505, CYP-CPR fusion protein (fatty acid hydroxylase) [<xref ref-type="bibr" rid="CR131">131</xref>].</p><p>Most aspergilli were found to contain two copies of CYP51, whereas only a single copy of CYP53 was present in all species. The fact that CYP53 is unique to filamentous fungi makes it an attractive candidate drug target against fungal pathogens [<xref ref-type="bibr" rid="CR131">131</xref>]. A series of inhibition experiments with ketoconazole (for CYP51) and benzoate (for CYP53) revealed complementary inhibition patterns for these CYPs, suggesting that simultaneous treatment with both drugs may be effective (Fig. <xref rid="Fig7" ref-type="fig">7</xref>). CYP61 was always present as a single ortholog, while surprisingly, CYP56 was not found in 11 species (Additional file <xref rid="MOESM13" ref-type="media">13</xref>A). As a part of an evolutionarily conserved gene cluster including CYP630, in most species a paralog, CPR2, was identified for the conserved main electron donor CPR1 (Additional file <xref rid="MOESM13" ref-type="media">13</xref>B). This cluster may be of importance when the main ß-oxidation pathway is overwhelmed by other substrates such as host terpenoid compounds [<xref ref-type="bibr" rid="CR129">129</xref>].<fig id="Fig7"><label>Fig. 7</label><caption><p>Molecular phylogenetic tree of (<bold>a</bold>) CYP51F1 (CYP51B) family and inhibition of growth on MBFA agar supplemented by 0.02 mM ketoconazole (K) and (<bold>b</bold>) CYP53 family and inhibition of growth on 2 mM benzoic acid (BA). Inhibition of growth (Inhib.) as per cent of the control without supplementation (Contr.) is shown in relation to phylogenetic trees, with growth culture plates shown to the <italic>right-hand side</italic> of the accompanying tree branch. Key to <italic>Aspergillus</italic> species: Aspfo = <italic>A. luchuensis</italic> (formerly <italic>A. foetidus</italic>); Asptu = <italic>A. tubingensis</italic>; Aspka = <italic>A. luchuensis</italic> (<italic>A. kawachii</italic>); Aspbr = <italic>A. brasiliensis</italic>; Aspni = <italic>A. nidulans</italic>; Aspca = <italic>A. carbonarius</italic>; Aspac = <italic>A. aculeatus</italic>; Aspfl = <italic>A. flavus</italic>; Aspor = <italic>A. oryzae</italic>; Aspwe = <italic>A. wentii</italic>; Aspcl; = <italic>A. clavatus</italic>; Aspfu = <italic>A. fumigatus</italic>; Neofi = <italic>A. fischeri</italic>; Aster = <italic>A. terreus</italic>; Aszo = <italic>A. zonatus</italic>; Asgl = <italic>A. glaucus</italic>; Aspsy = <italic>A. sydowii</italic>; Aspve = <italic>A. versicolor</italic></p></caption><graphic xlink:href="13059_2017_1151_Fig7_HTML" id="MO10"></graphic></fig></p><p>One to four copies of CYP-CPR fusion proteins were found in <italic>Aspergillus</italic> species. The presence of multiple copies may allow each particular fusion protein to function in a specific SM pathway. For the second type of fusion protein, haem peroxidase-CYP, orthologs of PpoA (CYP6001A subfamily) and PpoC (CYP6001C) were found in regions of colinearity in all genomes (except for <italic>A. zonatus</italic> and <italic>A. kawachii</italic>, respectively), implying conservation of biological function. Additional copies of haem peroxidase-CYP fusion proteins were present for some genomes in three different subgroups with homology either to PpoB from <italic>A. nidulans</italic>, PpoD from <italic>A. niger</italic> and <italic>A. flavus</italic>, or PpoB from <italic>A. fumigatus</italic> and <italic>A. flavus</italic> (Additional file <xref rid="MOESM14" ref-type="media">14</xref>). Specifically, the CYP6002A subfamily consists of PpoB from <italic>A. nidulans</italic> clustered together with orthologs from <italic>A. sydowii</italic>, <italic>A. versicolor</italic>, <italic>A. wentii</italic>, <italic>A. oryzae</italic>, <italic>A. terreus</italic>, <italic>A. clavatus</italic>, and <italic>A. fischeri</italic>. The CYP6003B subfamily consists of PpoD from <italic>A. niger</italic> and <italic>A. flavus</italic> and orthologs from <italic>A. glaucus</italic>, <italic>A. oryzae</italic>, <italic>A. terreus</italic>, <italic>A. tubingensis</italic>, <italic>A. luchuensi</italic>s, <italic>A. kawachii</italic>, and <italic>A. brasilensis</italic>. Finally, the CYP6001C subfamily comprises PpoB from <italic>A. fumigatus</italic> and <italic>A. flavus</italic> together with ortholgs from <italic>A. glaucus</italic>, <italic>A. terreus</italic>, <italic>A. oryzae</italic>, and <italic>A. fischeri</italic>.</p></sec></sec><sec id="Sec17"><title>Stress response</title><p>Filamentous fungi are exposed to a complex set of abiotic or biotic stresses in natural environments as well as in industrial processes where they are used to produce various biotechnological products. Effective stress perception and signal transduction mechanisms are necessary for adaptation and survival regardless of whether rapid or slow adaptation responses are required.</p><p>The complex and robust stress defense systems of the aspergilli [<xref ref-type="bibr" rid="CR132">132</xref>] were investigated using a wide array of stress physiology experimental and comparative genomics tools.</p><p>The stress tolerances of the aspergilli were screened under stress conditions including illumination, oxidative (H<sub>2</sub>O<sub>2</sub>, menadione), hyperosmotic (sorbitol, NaCl), heavy metal (Cd(II)), and cell wall integrity (calcofluor white, Congo Red) stress. The aspergilli were also exposed to selected antimycotics that interfere with cell wall (caspofungin) and cell membrane (voriconazole, amphotericin B) composition and structures. Stress sensitivities were tested in both liquid and surface cultures and the complete stress dataset with photographs is also available in the Fungal Stress Database [<xref ref-type="bibr" rid="CR133">133</xref>]. A more extensive description of the data can be found in Additional files <xref rid="MOESM3" ref-type="media">3</xref>, <xref rid="MOESM15" ref-type="media">15</xref>, <xref rid="MOESM16" ref-type="media">16</xref>, and <xref rid="MOESM17" ref-type="media">17</xref>.</p><sec id="Sec18"><title>Illumination <italic>stress</italic></title><p>Light-induced conidiation is common for most of the analyzed aspergilli. While light receptors and regulators were found to be conserved in most species (Additional file <xref rid="MOESM17" ref-type="media">17</xref>), rewiring of the response to the receptors and signal transduction pathways appears to have occurred in many species with respect to conidiation at different wavelengths. For example, blue or red light induced conidiation occurs in certain species but not others, while some species (e.g. <italic>A. versicolor</italic>) required specifically white light to induce sporulation. Interestingly, the industrially important black aspergilli and the opportunistic pathogens <italic>A. fumigatus</italic> and <italic>A. flavus</italic> showed little response to illumination (Fig. <xref rid="Fig8" ref-type="fig">8</xref>, Additional file <xref rid="MOESM17" ref-type="media">17</xref>).<fig id="Fig8"><label>Fig. 8</label><caption><p><bold>a</bold> Phylogenetic tree of <italic>Aspergillus</italic> species and summarized phenotypes from this study (modified from [<xref ref-type="bibr" rid="CR308">308</xref>]). All <italic>Aspergillus</italic> species were grown on malt extract agar (MEA) (<italic>blue</italic>) at 30 °C. <italic>Yellow squares</italic> stand for induced conidiation in white light. Abiotic and biotic stress determinants were colored in <italic>green</italic> for resistance (r), <italic>red</italic> for sensitive (s), <italic>no color</italic> for insensitive (-) and not determined (nd) different abiotic and biotic stressors: 2,4-diacetylphloroglucinol (DAPG), Hydrogen peroxide (OX), nitric oxide (NO), calcofluor white (CFW), caspofungin (CA), voriconazole (VO), amphotericin B (AmB), and <italic>Aspergillus</italic>-<italic>Pseudomonas fluorescens</italic> co-cultivation (Biotic). Species used in this study are framed in <italic>black</italic>. <bold>b</bold> Qualitative descriptive statistics of the exoproteome of four selected <italic>Aspergillus</italic> strains. Exoproteomes were enriched from filtered culture supernatants (<italic>Aspergillus</italic> MM, 30 °C) and analyzed by shotgun proteomics (LC-MS). Proteins were identified using draft genomic databases of the respective strains. For prediction of subcellular localization of the proteins the programs “SignaIP” and “WoLF PSORT” were used. For further analysis, sequences with an extracellular score >12 (WoLF PSORT) were defined as putatively secreted proteins (Additional file <xref rid="MOESM18" ref-type="media">18</xref>). Proteins with higher spectral count values after 0.2 mM hydrogen peroxide treatment (“upregulated after oxidative stress”) were selected statistically using MARVIS Filter (s/l > 0.5). <bold>c</bold> Exoproteomic heterogeneity in the genus <italic>Aspergillus</italic>. Comparative MARVIS cluster analysis of PFAM domains predicted in identified exoproteins (WoLF PSORT columns in bar chart B) of four selected <italic>Aspergillus</italic> species (WoLF PSORT: extracellular score >12) (Additional file <xref rid="MOESM19" ref-type="media">19</xref>). <italic>Colors</italic> represent the normalized frequency of occurrence of PFAM-domains in the respective exoproteome. Indicated by the color scale on the <italic>right</italic>, the color scale ranges from <italic>blue</italic> (no domain) via <italic>green</italic> (few domains) to <italic>red</italic> (more domains). Each <italic>column</italic> of the cluster image resembles one PFAM-domain. The proteome data is available at <ext-link ext-link-type="uri" xlink:href="http://wwwuser.gwdg.de/~hkusch/GBIO_DeVries/">http://wwwuser.gwdg.de/~hkusch/GBIO_DeVries/</ext-link></p></caption><graphic xlink:href="13059_2017_1151_Fig8_HTML" id="MO11"></graphic></fig></p></sec><sec id="Sec19"><title>Oxidative stress</title><p>In solid media experiments, <italic>A. brasiliensis</italic> showed outstanding menadione tolerance, which correlated with the emergence of two putative new-type SodA superoxide dismutases (Fig. <xref rid="Fig9" ref-type="fig">9</xref>). In liquid cultures, <italic>A. carbonarius</italic> and <italic>A. niger</italic> CBS113.46 were especially resistant to high oxidative stress provided by hydrogen peroxide while <italic>A. zonatus</italic> and <italic>A. sydowii</italic> were the most sensitive species (Fig. <xref rid="Fig8" ref-type="fig">8</xref>). In the case of <italic>A. carbonarius</italic>, the remarkable H<sub>2</sub>O<sub>2</sub> tolerance was coupled to the co-occurrance of two C-type—one group cIII and one group cIV—catalases (Additional file <xref rid="MOESM15" ref-type="media">15</xref>). The catalase-encoding <italic>catC</italic> gene (coding for group cIV catalase; Additional file <xref rid="MOESM15" ref-type="media">15</xref>) has been lost in some <italic>Aspergillus</italic> genomes including <italic>A. fischeri</italic>, <italic>A. clavatus</italic>, and <italic>A. fumigatus</italic>. In the latter species, the <italic>easC</italic> gene for ergot synthesis (a group cIII catalase gene, Additional file <xref rid="MOESM15" ref-type="media">15</xref>) [<xref ref-type="bibr" rid="CR134">134</xref>] appears to have taken over protective functions against oxidative stress (Additional files <xref rid="MOESM15" ref-type="media">15</xref> and <xref rid="MOESM17" ref-type="media">17</xref>).<fig id="Fig9"><label>Fig. 9</label><caption><p>Linking species-level differences in selected <italic>Aspergillus</italic> stress-defense proteins to major stress tolerance phenotypes. The remarkable Cd(II) tolerance of <italic>A. fumigatus</italic> and <italic>A. sydowii</italic> (<bold>a</bold>), the outstanding menadione sodium bisulfite (MSB) tolerance of <italic>A. brasiliensis</italic> (<bold>b</bold>) and the osmophility of <italic>A. glaucus</italic> and <italic>A. wentii</italic> (<bold>c</bold>) were attributed to variations in the cadmium transporting P-type ATPases (<bold>a</bold>), Cu/Zn-superoxide dismutases (<bold>b</bold>), and NAD-dependent glycerol-3-phosphate dehydrogenases (<bold>c</bold>), respectively. In this Figure, the stress sensitivities of <italic>A. nidulans</italic> are also presented for comparison (<bold>a</bold>–<bold>c</bold>), although this species lacks any Pca1 ortholog (Additional file <xref rid="MOESM15" ref-type="media">15</xref>). In the dendograms, putative orthologs of baker’s yeast Pca1 cadmium transporting P-type ATPase (<bold>a</bold>), <italic>Aspergillus nidulans</italic> SodA Cu/Zn-superoxide dismutase (<bold>b</bold>), and <italic>A. nidulans</italic> GfdA/B NAD-dependent glycerol-3-phosphate dehydrogenases (<bold>c</bold>) are shown. In (<bold>c</bold>), <italic>S. cerevisiae</italic> Gpd1/2 paralogs are also presented. Putative <italic>A. sydowii</italic> (<inline-graphic xlink:href="13059_2017_1151_Figa_HTML.gif" id="d29e6396"></inline-graphic>) and <italic>A. fumigatus</italic> (<inline-graphic xlink:href="13059_2017_1151_Figb_HTML.gif" id="d29e6402"></inline-graphic>) Pca1 orthologs (<bold>a</bold>) and putative <italic>A. glaucus</italic> (<inline-graphic xlink:href="13059_2017_1151_Figc_HTML.gif" id="d29e6412"></inline-graphic>) and <italic>A. wentii</italic> (<inline-graphic xlink:href="13059_2017_1151_Figd_HTML.gif" id="d29e6418"></inline-graphic>) GfdA orthologs (<bold>c</bold>) are indicated by <italic>symbols</italic> presented in the <italic>parentheses</italic>. Hypothetical new-type SodA enzymes found in <italic>A. brasiliensis</italic> are indicated by <italic>red lines</italic> in (<bold>b</bold>). Pca1, SodA, and GfdA/B orthologs are indicated by four-letter species name identifiers (listed in Additional file <xref rid="MOESM15" ref-type="media">15</xref>) and locus IDs as found in AspGD (<ext-link ext-link-type="uri" xlink:href="http://www.aspergillusgenome.org/">http://www.aspergillusgenome.org/</ext-link>) for the aspergilli. The relevant JGI locus IDs are listed in Additional file <xref rid="MOESM16" ref-type="media">16</xref>. The Gpd1/2 paralogs of budding yeast are from the <italic>Saccharomyces</italic> Genome Database (<ext-link ext-link-type="uri" xlink:href="http://www.yeastgenome.org/">http://www.yeastgenome.org/</ext-link>). <italic>Photographs</italic> on the tress tolerance/sensitivity phenotypes were taken from the Fungal Stress Database (<ext-link ext-link-type="uri" xlink:href="http://www.fung-stress.org/">http://www.fung-stress.org/</ext-link>). Further details of the phylogenetic and evolutionary calculations and more information on the stress response proteins can be found in Additional file <xref rid="MOESM15" ref-type="media">15</xref></p></caption><graphic xlink:href="13059_2017_1151_Fig9_HTML" id="MO12"></graphic></fig></p></sec><sec id="Sec20"><title>Hyperosmotic stress</title><p>One of the most interesting outcomes of the stress studies was that osmophily was more widespread in the genus <italic>Aspergillus</italic> than previously thought. Experimental evidence was obtained for osmophily in <italic>A. glaucus</italic>, <italic>A. wentii</italic>, <italic>A. versicolor</italic>, <italic>A. sydowii</italic>, and <italic>A. oryzae</italic> (Additional file <xref rid="MOESM3" ref-type="media">3</xref>). In the case of <italic>A. glaucus</italic> and <italic>A. wentii</italic>, osmophily correlated with the lack of GfdB, a putative NAD<sup>+</sup>-dependent glycerol-3-phosphate dehydrogenase, with a predicted function in glycerol metabolism (Fig. <xref rid="Fig9" ref-type="fig">9</xref>; Additional file <xref rid="MOESM15" ref-type="media">15</xref>). This is consistent with previous work in <italic>A. nidulans</italic> showing that elimination of <italic>gfdA</italic>, which also encodes a putative glycerol metabolic enzyme, led to an osmoremediable phenotype in the presence of 1 M NaCl (Additional files <xref rid="MOESM3" ref-type="media">3</xref> and <xref rid="MOESM15" ref-type="media">15</xref>) [<xref ref-type="bibr" rid="CR135">135</xref>].</p></sec><sec id="Sec21"><title>Heavy metal stress</title><p>Cd(II) tolerance was clearly correlated with the presence of a Pca1-type Cd(II) transporter in the studied genomes (Fig. <xref rid="Fig9" ref-type="fig">9</xref>, Additional files <xref rid="MOESM3" ref-type="media">3</xref> and <xref rid="MOESM15" ref-type="media">15</xref>). Not surprisingly, <italic>A. sydowii</italic>, <italic>A. fumigatus</italic>, <italic>A. wentii</italic>, <italic>A. versicolor</italic>, and <italic>A. terreus</italic>, all harboring a Pca1 ortholog, were the most tolerant to Cd(II). Interestingly, the important opportunistic human pathogen <italic>A. fumigatus</italic> also possessed high Cd(II) tolerance, but it was remarkably sensitive to oxidative, osmotic, and cell wall integrity stress when compared to other aspergilli (Fig. <xref rid="Fig9" ref-type="fig">9</xref>, Additional files <xref rid="MOESM3" ref-type="media">3</xref> and <xref rid="MOESM15" ref-type="media">15</xref>).</p></sec><sec id="Sec22"><title>Cell wall integrity stress and sensitivity to antimycotics</title><p>The cell walls of the aspergilli consist of chitin, β-1,3-glucan, β-1,6-glucan, α-1,3-glucan, galactomannan, and galactosaminogalactan. Genes required for the synthesis and remodeling of these polymers were found in all sequenced <italic>Aspergillus</italic> genomes, although a high degree of redundancy was observed (Additional file <xref rid="MOESM17" ref-type="media">17</xref>). The number of chitin synthases was in the range of 9–15 (noting that <italic>S. cerevisiae</italic> only harbors three chitin synthases). The number of chitin remodeling, chitin-glucan crosslinking, and β-glucan synthesis enzymes also differed considerably (21–31, 10–18, and 15–31, respectively). No such extreme differences were observed with respect to galactomannan and galactosaminogalactan synthesis. However, there was no correlation between the number of cell wall genes and overall susceptibility to the cell wall acting drugs calcofluor white, Congo Red, and caspofungin (Fig. <xref rid="Fig8" ref-type="fig">8</xref>, Additional files <xref rid="MOESM15" ref-type="media">15</xref> and <xref rid="MOESM17" ref-type="media">17</xref>). In addition, voriconazole and amphotericin B, which affect the composition and structure of cell membranes, also showed species-specific effects (Additional file <xref rid="MOESM17" ref-type="media">17</xref>). Therefore, it is likely that numerous strategies have evolved in different <italic>Aspergillus</italic> species to counteract the presence of these antifungals, as has previously been suggested [<xref ref-type="bibr" rid="CR136">136</xref>].</p></sec></sec><sec id="Sec23"><title>Transporters</title><p>The complex mixtures of nutrients found in natural growth substrates require transport across cell membranes in order to be assimilated into the fungal cell. To analyze genes that encode transporters, 19 <italic>Aspergillus</italic> genomes were compared to 16 genomes of other fungi, resulting in the detection of up to 120 different transporter-related Pfam motifs in at least one species. The total number of transporters identified in the genomes varied dramatically from 301 transporter-encoding open reading frames (ORFs) in <italic>Schizosaccharomyces pombe</italic> to 1601 in <italic>A. versicolor</italic>. The number of ORFs contributing to the transportome of members of the Eurotiomycetes was variable, the lowest number being 810 in <italic>A. clavatus</italic>, which is still more than twice the number found in the yeasts <italic>S. pombe</italic> or <italic>Saccharomyces cerevisiae</italic>. The majority of transporter types (as denoted by the presence of the Pfam motifs) are present in similar numbers in the genomes of all the fungi included in this study. The Major Facilitator Superfamily, which contributes the largest number of ORFs to the transportome, is also the transporter class showing the highest level of expansion in the Eurotiomyces, with the ABC transporter superfamily also showing a noticeable increase. This expansion of the transporter capacity of the fungi correlates with the ability to use a greater diversity of substrates. The redundancy of most transport systems renders the study of fungal transporters a complex topic where much remains to be discovered. Some subclasses of transporters are discussed in more detail below.</p><sec id="Sec24"><title>The Aspergillus sugar transportome</title><p>Sugars are not only important nutrients and structural precursors but are also signaling molecules that trigger changes in gene regulation. Sugar transport and sensing are therefore crucial functions in fungal cells and considerable progress in understanding the molecular bases of these processes has been made in studies on yeast [<xref ref-type="bibr" rid="CR137">137</xref>]. Most sugar transporters belong to the Major Facilitator Superfamily (MFS) [<xref ref-type="bibr" rid="CR138">138</xref>, <xref ref-type="bibr" rid="CR139">139</xref>] of secondary transporters (secondary active transporters and facilitators), which currently comprises 82 named classes [<xref ref-type="bibr" rid="CR140">140</xref>, <xref ref-type="bibr" rid="CR141">141</xref>]. In order to investigate the sugar transporter complements of diverse filamentous fungi, we focused on those proteins from <italic>Aspergillus</italic> species that were classified as members of the PFAM family of “Sugar and other transporters” (PF00083). Most, but not all, members of this family catalyze sugar transport, with their substrates including hexoses, pentoses, disaccharides, alpha-glucosides, inositol, and quinic acid as well as organic and inorganic ions.</p><p>Using the annotated genome data from eight previously available <italic>Aspergillus</italic> species, a total of 940 putative PF00083 transporters were identified after manual filtering and reannoation to yield greater consensus to the conserved 12 transmembrane domain topology. From phylogenetic analysis, the vast majority of sequences were found to fall into eight major clades (A to H; Fig. <xref rid="Fig10" ref-type="fig">10</xref>). Although support for the very basal branches is generally low, the subclades within them have high bootstrap support.<fig id="Fig10"><label>Fig. 10</label><caption><p>Overview of sugar transporters. The evolutionary history of 940 PF00083 sequences identified in the genomes of <italic>A. clavatus</italic>, <italic>A. flavus</italic>, <italic>A. fumigatus</italic>, <italic>A. nidulans</italic>, <italic>A. niger</italic>, <italic>A. oryzae</italic>, <italic>A. terreus</italic>, and <italic>A. fischeri</italic> was inferred using the neighbor-joining method. The optimal tree is shown. Nodes with 50–69% (∆) or 70–100% (○) bootstrap support (1000 replicates) are indicated. Evolutionary distances were computed using the Poisson correction method and are in the units of the number of amino acid substitutions per site. All ambiguous positions were removed for each sequence pair. Evolutionary analyses were conducted in MEGA6. A small number of sequences could not be assigned to the main clades identified; referring to the smallest genome analyzed (<italic>A. clavatus</italic>), these correspond to <italic>loci</italic> ACLA023780, ACLA026890, ACLA031920, and ACLA041390. Potential substrates for members of the clades are suggested based on experimentally determined transporter functions</p></caption><graphic xlink:href="13059_2017_1151_Fig10_HTML" id="MO13"></graphic></fig></p><p>This initial analysis was extended to include an additional 1422 sequences corresponding to the PF00083 complements of the novel <italic>Aspergillus</italic> genomes, along with those of two fungi for which experimental evidence of function has been obtained for a number of PF00083 members: <italic>N. crassa</italic> (Sordariomycete) and <italic>S. cerevisiae</italic>. For comparison, the complements of <italic>P. chrysogenum</italic>, <italic>T. marneffei</italic>, <italic>T. reesei</italic>, and two animal pathogens (<italic>Histoplasma capsulatum</italic> and <italic>Microsporum canis</italic>) were also included. Additional files <xref rid="MOESM20" ref-type="media">20</xref> and <xref rid="MOESM21" ref-type="media">21</xref> present a summary and details, respectively, of the numbers and distribution of PF00083 members found in each of the clades and the function(s) identified for some members of those clades. Considerable diversity in the numbers of PF00083 members was found, with a threefold difference existing between those species having the largest and smallest complements (<italic>A. sydowii</italic> vs. <italic>A. clavatus</italic>). Even species from the same sections do not have very similar numbers of loci, for example: members of the <italic>Nigri</italic> range from 83 to 113. Of the <italic>Nidulanti</italic>, <italic>A. sydowii</italic> (180) and <italic>A. versicolor</italic> (171) have the highest numbers of loci whereas the number present in <italic>A. nidulans</italic> (113) is similar to that observed in <italic>A. niger</italic> and <italic>P. chrysogenum</italic>. The three genome-sequenced <italic>A. niger</italic> strains (consisting of an enzyme producer, a citric acid producer, and a laboratory strain) all have similar PF00083 complements. Perhaps surprisingly, <italic>T. reesei</italic> (Sordariomycete), a well-known producer of plant cell wall degrading enzymes, only has 64 members. Interestingly, <italic>A. clavatus</italic> has a very similar complement size (63) but there is a notable enrichment of <italic>T. reesei</italic> members in clade D and a reduction in clade G compared to <italic>A. clavatus. A. terreus</italic> (123) and <italic>A. wentii</italic> (120) also have similar numbers of PF00083 members but clade D is threefold enriched in the former, while <italic>A. wentii</italic>, along with <italic>A. sydowii</italic> and <italic>A. versicolor</italic>, has the highest number of members of clade F. To evaluate transporter function in the different clades, we combined data from the literature with results from studies involving the functional complementation of <italic>S. cerevisiae</italic> sugar transporter mutants with 43 putative transporters from <italic>A. niger</italic> (Additional file <xref rid="MOESM22" ref-type="media">22</xref>).</p><p>Clade A comprises three distinct subclades (bootstrap values >90%) and experimental data demonstrated the transport of certain monosaccharides for a number of its members. Both high-affinity and low-affinity glucose transporters of <italic>A. nidulans</italic> (HxtC, HxtE, MstA, MstC, and MstE), <italic>A. niger</italic> (MstA, MstC), and <italic>N. crassa</italic> (Hgt-1, Glt-1) are found in subclade A(i), as well as two broad-specificity transporters of glucose/pentoses (An29-2, Xyt-1) [<xref ref-type="bibr" rid="CR138">138</xref>, <xref ref-type="bibr" rid="CR139">139</xref>, <xref ref-type="bibr" rid="CR142">142</xref>–<xref ref-type="bibr" rid="CR147">147</xref>]. Paralogous high-affinity glucose transporters (MstA and MstC) differing in their patterns of expression are present in <italic>A. nidulans</italic> [<xref ref-type="bibr" rid="CR144">144</xref>]. This duplication is also found in the other two <italic>Nidulantes</italic> (in fact <italic>A. sydowii</italic> has three loci, as does <italic>N. crassa</italic>) but is absent in all the other aspergilli analyzed here. <italic>A. glaucus</italic> lacks MstA/MstC homologs. Analysis of the <italic>A. niger</italic> transporters indicated the ability to transport D-glucose, D-galactose, and D-mannose for all tested proteins, while all but one were also able to transport D-fructose (Additional file <xref rid="MOESM22" ref-type="media">22</xref>).</p><p>An <italic>N. crassa</italic> transporter (Lat-1) of broad sugar substrate specificity (arabinose and other sugars) and a closely related arabinose-specific transporter from <italic>Myceliophthora thermophila</italic> (MtLat-1) map to subclade A(ii) [<xref ref-type="bibr" rid="CR148">148</xref>], as does the HxtA protein of <italic>A. nidulans</italic> [<xref ref-type="bibr" rid="CR149">149</xref>]. The tested <italic>A. niger</italic> transporters of this group showed broad specificity, covering the monosaccharaides and oligosaccharides D-glucose, D-mannose, D-fructose, D-galactose, maltose, melizitose, and turanose (Additional file <xref rid="MOESM22" ref-type="media">22</xref>).</p><p><italic>A. nidulans</italic> and <italic>N. crassa</italic> xylose transporters [<xref ref-type="bibr" rid="CR150">150</xref>, <xref ref-type="bibr" rid="CR151">151</xref>] occur in subclade A(iii). While one of the tested <italic>A. niger</italic> transporters from this subclade appeared to be specific for D-glucose, the others are more similar in their specificities to the members of subclade A(i) (Additional file <xref rid="MOESM22" ref-type="media">22</xref>). One member is also able to transport the disaccharides maltose and trehalose. Clade A might therefore be considered to comprise three diverse groupings of predominantly pentose/hexose transporters.</p><p>Clade B contains quinic acid [<xref ref-type="bibr" rid="CR152">152</xref>, <xref ref-type="bibr" rid="CR153">153</xref>] and D-galacturonic acid (GAT-1, GatA) [<xref ref-type="bibr" rid="CR154">154</xref>, <xref ref-type="bibr" rid="CR155">155</xref>] transporters. GatA homologs are present in most aspergilli except section <italic>Fumigati</italic>, <italic>A. clavatus</italic>, and <italic>A. zonatus</italic>. By contrast, no GAT-1 homologs are present in section <italic>Nigri</italic>, <italic>A. glaucus</italic>, or <italic>A. zonatus</italic>. Analysis of <italic>A. niger</italic> members of this clade only revealed the ability to transport D-glucose for some members (Additional file <xref rid="MOESM22" ref-type="media">22</xref>).</p><p>Clade C comprises three major subclades supported by very high bootstrap values. Subclade C(i) contains homologs of the <italic>S. cerevisiae</italic> inositol transporters Itr1 and Itr2 [<xref ref-type="bibr" rid="CR156">156</xref>] and the putative <italic>Cryptococcus neoformans</italic> inositol transporters [<xref ref-type="bibr" rid="CR157">157</xref>]. Subclade C(ii) members show homology to the fructose transporters Fsy1 and Frt1 identified in <italic>S. pastorianus (carlsbergensis)</italic> and <italic>Botrytis cinerea</italic>, respectively [<xref ref-type="bibr" rid="CR158">158</xref>, <xref ref-type="bibr" rid="CR159">159</xref>]. Clade C(iii) comprises homologs corresponding to “group 2” putative inositol transporters [<xref ref-type="bibr" rid="CR157">157</xref>] that are related to the putative inositol transporter Hgt19 of <italic>Candida albicans</italic> [<xref ref-type="bibr" rid="CR160">160</xref>]. The <italic>A. niger</italic> members of this clade revealed highly diverse abilities to transport monosaccharides and/or oligosaccharides (Additional file <xref rid="MOESM22" ref-type="media">22</xref>).</p><p>Clade D incorporates oligosaccharide transporters including the <italic>A. oryzae</italic> maltose permease MalP and its homolog [<xref ref-type="bibr" rid="CR161">161</xref>], homologs of the melibiose transporter MBT1 of <italic>Colletotrichum graminicola</italic> [<xref ref-type="bibr" rid="CR162">162</xref>], the maltose transporters of <italic>S. cerevisiae</italic> (Mal11, Mal31, Mal61, and Mph3) [<xref ref-type="bibr" rid="CR137">137</xref>], and MRT of <italic>Metarhizium robertsii</italic> [<xref ref-type="bibr" rid="CR163">163</xref>]. Similar to Clade C, highly diverse abilities of the tested <italic>A. niger</italic> members of this clade were observed (Additional file <xref rid="MOESM22" ref-type="media">22</xref>).</p><p>Clade E can be divided into two main subclades: E(i) contains homologs of phosphate transporters [<xref ref-type="bibr" rid="CR164">164</xref>–<xref ref-type="bibr" rid="CR166">166</xref>] and the <italic>S. cerevisiae</italic> transporter (GIT1) of glycerophosphoinositol and glycerophosphocholine [<xref ref-type="bibr" rid="CR167">167</xref>], while members of E(ii) share homology with the <italic>S. cerevisiae</italic> monocarboxylic acid/selenite transporter Jen1 [<xref ref-type="bibr" rid="CR168">168</xref>]. No <italic>A. niger</italic> members of this clade have been characterized.</p><p>Clade F contains the yeast glycerol transporter Stl1 [<xref ref-type="bibr" rid="CR169">169</xref>], the <italic>N. crassa</italic> pentose permease XAT-1 [<xref ref-type="bibr" rid="CR145">145</xref>], and the xylose specific permease An25 [<xref ref-type="bibr" rid="CR151">151</xref>]. Several of the <italic>A. niger</italic> members of this clade were able to transport oligosaccharides, while others appeared to be specific for glycerol or mannitol (Additional file <xref rid="MOESM22" ref-type="media">22</xref>).</p><p>No homology to a functionally characterized transporter has been observed for any members of clade G. However, one of the tested <italic>A. niger</italic> members was able to transport D-glucose while another transported maltose, trehalose, and melizitose.</p><p>Clade H contains the <italic>A. nidulans</italic> lactose permeases LacpA and LacpB [<xref ref-type="bibr" rid="CR170">170</xref>, <xref ref-type="bibr" rid="CR171">171</xref>] and <italic>N. crassa</italic> cellodextrin transporters [<xref ref-type="bibr" rid="CR172">172</xref>, <xref ref-type="bibr" rid="CR173">173</xref>]. One of the tested <italic>A. niger</italic> members was able to transport melizitose and turanose (Additional file <xref rid="MOESM22" ref-type="media">22</xref>).</p><p>It is unclear if the widespread occurrence of broad-specificity transporters in <italic>A. niger</italic>, as indicated by the functional complementation studies in <italic>S. cerevisiae</italic>, is specific to this species or common among a wider range of fungi. A transportome containing a diversity of broad-specificity sugar transporters is congruent with a saprobic lifestyle where degradation of natural substrates provides complex mixtures of monosaccharides, disaccharides, and trisaccharides.</p></sec><sec id="Sec25"><title>Amino acid transporters</title><p>Phylogenetic analysis (Additional file <xref rid="MOESM23" ref-type="media">23</xref>) makes it possible to propose which paralogs are responsible for the uptake of aromatic amino acids (two clades, shown in purple) and those responsible for the uptake of basic amino acids (shown in red). This analysis suggests that, in some cases, specificity arose prior to the divergence of the Saccharomycotina and the Pezizimycotina (e.g. for basic and di-carboxylic amino acids, and for proline) while in other cases the amino acid specificity evolved later. The <italic>S. cerevisiae</italic>-specific subclade shown in light orange is suggested to be a group of broad specificity permeases (excluding proline) based on their similarity to <italic>N. crassa pmg</italic> and its possible ortholog from <italic>Trichoderma harzianum</italic> [<xref ref-type="bibr" rid="CR174">174</xref>, <xref ref-type="bibr" rid="CR175">175</xref>]. The clade clustering with Tat3 of <italic>Saccharomyces pastorianus</italic> (deep purple) [<xref ref-type="bibr" rid="CR176">176</xref>] may indicate a specificity for aromatic amino acids, while the ability to transport cystine is indicated by the <italic>Candida glabrata</italic> gene <italic>YAT</italic> [<xref ref-type="bibr" rid="CR177">177</xref>]. A clade, shown in blue contains the well-characterized proline permease of <italic>A. nidulans</italic> ([<xref ref-type="bibr" rid="CR178">178</xref>] and references therein), clustered with its ortholog, Put4 from <italic>S. cerevisiae</italic>; similarly the <italic>S. cerevisiae</italic> aspartate/glutamate transporter Dip5 is an outgroup of a clade shown in green which contains the isofuctional ortholog of <italic>A. nidulans</italic> [<xref ref-type="bibr" rid="CR179">179</xref>].</p><p>A recent study [<xref ref-type="bibr" rid="CR180">180</xref>] has allowed us to predict that the smaller clade (shown in red) represents lysine-specific permeases while the larger clade (also shown in red; including AN8279) probably transports arginine and other basic amino acids. Interestingly, AN8279, possessing a Ser residue in TMS10, resembles the T456S mutant of Can1, suggesting that AN8279 is a high affinity and high capacity transporter for both arginine and lysine. A detailed study of the substrate specificity determinants of the <italic>A. nidulans</italic> PrnB transporter suggested that substrate specificity of this family is largely determined by residues in certain key transmembrane domains [<xref ref-type="bibr" rid="CR178">178</xref>, <xref ref-type="bibr" rid="CR181">181</xref>].</p><p>The aspergilli screened were found to possess variable numbers of AAAP (Amino Acid/Auxin Permease) family members (TCDB 2.A.18) [<xref ref-type="bibr" rid="CR140">140</xref>] and some <italic>S. cerevisiae</italic> AAAP proteins have been described as bi-directional vacuolar amino acid transporters, with some shown to be broad specificity permeases accepting aromatic and aliphatic amino acids [<xref ref-type="bibr" rid="CR182">182</xref>]. All aspergilli were found to possess at least one methionine transporter.</p></sec><sec id="Sec26"><title>Urea transporters</title><p>Urea is taken up by fungi and plants through a group of active urea/H<sup>+</sup> symporters, belonging to the sodium:solute symporter family (SSS), as typified by <italic>A. nidulans</italic> UreA [<xref ref-type="bibr" rid="CR183">183</xref>, <xref ref-type="bibr" rid="CR184">184</xref>] With the exception of <italic>A. zonatus</italic>, which has only one homolog, the <italic>Aspergillus</italic> genomes were found to contain a range of 2–7 UreA homologs, most of which are predicted to have 15 transmembrane segments (TMSs) (Table <xref rid="Tab5" ref-type="table">5</xref>). The phylogenetic relationships of the UreA homologs suggest that two duplication events occurred before the different <italic>Aspergillus</italic> species diverged from a common ancestor, giving rise to two clades (Additional file <xref rid="MOESM24" ref-type="media">24</xref>). The first sub-clade, which contains UreA, also contains an ortholog from each of the fungi analyzed, suggesting conservation of urea transport function. The second clade contains members that have not yet been functionally characterized.<table-wrap id="Tab5"><label>Table 5</label><caption><p>Number of UreA homologs found in the analyzed aspergilli. In <italic>A. niger</italic>, <italic>A. luchuensis</italic>, and <italic>A. fumigatus</italic>, the same number of homologs were found in each of the two sequenced strains</p></caption><table frame="hsides" rules="groups"><thead><tr><th>Species</th><th>UreA homologs (<italic>n</italic>)</th><th>Species</th><th>UreA homologs (<italic>n</italic>)</th></tr></thead><tbody><tr><td><italic>A. niger</italic></td><td>4</td><td><italic>A. oryzae</italic></td><td>3</td></tr><tr><td><italic>A. luchuensis</italic></td><td>4</td><td><italic>A. flavus</italic></td><td>3</td></tr><tr><td><italic>A. tubingensis</italic></td><td>3</td><td><italic>A. terreus</italic></td><td>4</td></tr><tr><td><italic>A. brasiliensis</italic></td><td>4</td><td><italic>A. fumigatus</italic></td><td>3</td></tr><tr><td><italic>A. carbonarius</italic></td><td>4</td><td><italic>A. fischeri</italic></td><td>3</td></tr><tr><td><italic>A. aculeatus</italic></td><td>2</td><td><italic>A. clavatus</italic></td><td>3</td></tr><tr><td><italic>A. versicolor</italic></td><td>7</td><td><italic>A. glaucus</italic></td><td>4</td></tr><tr><td><italic>A. sydowii</italic></td><td>5</td><td><italic>A. wentii</italic></td><td>5</td></tr><tr><td><italic>A. nidulans</italic></td><td>4</td><td><italic>A. zonatus</italic></td><td>1</td></tr></tbody></table></table-wrap></p><p>Amino acid residues important for the binding, recognition, and/or translocation of urea and for the sorting of UreA to the membrane were recently identified [<xref ref-type="bibr" rid="CR185">185</xref>]. All of these residues are conserved in all UreA orthologs of the genus, with the exception of <italic>A. aculeatus</italic> where an alanine (Ala163 in UreA) is substituted by a serine. This is remarkable since there is a Ser present at the corresponding position in characterized UreA orthologs of <italic>S. cerevisiae</italic>, <italic>C. albicans</italic>, and <italic>P. involutus</italic> [<xref ref-type="bibr" rid="CR185">185</xref>].</p></sec><sec id="Sec27"><title>Nitrate, nitrite, and ammonium transporters</title><p>All sequenced aspergilli were found to possess at least one copy of the <italic>nrtA</italic> gene encoding a Nitrate Nitrite Porter (NNP, TCDB 2.A.1.8) [<xref ref-type="bibr" rid="CR140">140</xref>] protein for nitrate/nitrite transport [<xref ref-type="bibr" rid="CR186">186</xref>–<xref ref-type="bibr" rid="CR188">188</xref>]. This conserved nitrate transporter-encoding gene is located in a cluster with genes for nitrite reductase and nitrate reductase. <italic>Aspergillus nidulans</italic>, <italic>A. fumigatus</italic>, and <italic>A. fischeri</italic> also have a second nitrate transporter located outside the cluster. In <italic>A. nidulans</italic>, it has been shown that the two transporters, NrtA (in the cluster with nitrate and nitrite reductases) and NrtB, are expressed under identical conditions but have different affinities for nitrate and nitrite, suggesting a kinetic flexibility that may confer an advantage to the species growing in its natural habitat in soil where substrate concentrations can vary rapidly by orders of magnitude [<xref ref-type="bibr" rid="CR189">189</xref>, <xref ref-type="bibr" rid="CR190">190</xref>]. NrtA displays low affinity, high capacity while NrtB is a high affinity, low capacity protein. In species with a single NNP, the protein more closely resembles NrtA rather than NrtB using a Smith-Waterman algorithm for pairwise comparison (Additional file <xref rid="MOESM25" ref-type="media">25</xref>).</p><p>Nitrite transport can also be performed by proteins of the formate-nitrite transporter (FNT) family (PF01226; TCDB 2.A.44) [<xref ref-type="bibr" rid="CR140">140</xref>]. Bioinformatic analysis in the present study revealed that the majority of the aspergilli contain one gene encoding an FNT family protein, but a few species (<italic>A. flavus</italic>, <italic>A. oryzae</italic>, <italic>A. sidowii</italic>, <italic>A. fischeri</italic>, and <italic>A. versicolor</italic>) have two such genes. In <italic>A. nidulans</italic>, the FNT protein NitA has been shown to be a high affinity but low capacity nitrite transporter compared to NNP proteins and is expressed under the same conditions as the NNP proteins [<xref ref-type="bibr" rid="CR191">191</xref>].</p><p>The aspergilli also contain one to six members of the proton-dependent oligopeptide transporter (PTR) family (PF00854: TCDB 2.A.17) [<xref ref-type="bibr" rid="CR140">140</xref>] that includes the <italic>Arabidopsis thaliana</italic> nitrate transporter, Nrt1.1 (CHL1). However, absence of the nitrate binding residues identified in Nrt1.1 (H356 and Y388) [<xref ref-type="bibr" rid="CR192">192</xref>, <xref ref-type="bibr" rid="CR193">193</xref>] implies that nitrate transport by PTR family proteins in the aspergilli is unlikely.</p><p>The aspergilli usually possess three or four members of the ammonium transporter/methylammonium permease/Rhesus factor family (AMT/MEP/Rh family) (PF00909; TCDB 1.A.11.2) [<xref ref-type="bibr" rid="CR140">140</xref>], although the <italic>A. zonatus</italic> genome contains five genes encoding such proteins. In <italic>A. nidulans</italic>, these genes are differentially regulated with MeaA being the principle ammonium transporter in conditions where ammonium is non-limiting. By contrast, MepA is expressed under nitrogen limiting and nitrogen starvation conditions and MepB is only expressed during complete nitrogen starvation [<xref ref-type="bibr" rid="CR194">194</xref>]. MepA and MepB display higher substrate affinity than MeaA [<xref ref-type="bibr" rid="CR194">194</xref>].</p><p>The inorganic nitrogen transport capability emphasized by the present study most likely reflects the natural habitat of <italic>Aspergillus</italic> species in the soil where nitrate, nitrite, and ammonium form the principle inorganic salts of nitrogen. The diversity of transporters detected is of applied significance as it indicates flexibility in terms of the inorganic nitrogen sources that can be provided for growth of biotechnologically important aspergilli. However, for nitrate utilization (and by extension nitrite utilization), uptake of nitrate has generally been considered a “bottleneck” and so the manipulation of gene copy number in strains could be a goal for strain improvement. On undefined industrial media used for growing fungi, there may be scope for higher biomass yields and faster growth by manipulating inorganic nitrogen transporters.</p></sec><sec id="Sec28"><title>Nucleobase and nucleoside transporters</title><p>There are two main fungal families specific for nucleobase and one for nucleoside uptake as described below. In addition, a fourth family, the Equilibrative Nucleoside Transporter (ENT)-like family (2.A.57) [<xref ref-type="bibr" rid="CR140">140</xref>], with a similarity to nucleoside transporters of protozoa and metazoa, is also present in fungi but has not been characterized [<xref ref-type="bibr" rid="CR195">195</xref>]. Some of these transporters (e.g. NCS1 and AzgA; see below) are ubiquitous in fungi but absent in mammals, which makes them promising candidates for designing novel targeted pharmacologic agents against pathogenic fungi [<xref ref-type="bibr" rid="CR196">196</xref>].</p><sec id="FPar1"><title>Nucleobase Ascorbate Transporter family</title><p>Homologs of the Nucleobase Ascorbate Transporter (NAT) family (or Nucleobase Cation Symporter NCS2 family, 2.A.40) [<xref ref-type="bibr" rid="CR140">140</xref>] are present in all domains of life and most fungi [<xref ref-type="bibr" rid="CR197">197</xref>–<xref ref-type="bibr" rid="CR199">199</xref>]. Members are thought to consist of 14 transmembrane domains (TMD) and have extended cytoplasmic N-tails and C-tails [<xref ref-type="bibr" rid="CR200">200</xref>]. Fungal NATs can be further classified intro three distinct subfamilies based on their specificity and primary sequences. First are the “canonical” UapA/C group [<xref ref-type="bibr" rid="CR201">201</xref>, <xref ref-type="bibr" rid="CR202">202</xref>], which are uric acid/xanthine/H+ symporters [<xref ref-type="bibr" rid="CR203">203</xref>–<xref ref-type="bibr" rid="CR205">205</xref>]. UapC-like homologs were found to be syntenic and present in all species of aspergilli in the present study (and duplicated in some) [<xref ref-type="bibr" rid="CR206">206</xref>], whereas UapA paralogues were present only in <italic>A. nidulans</italic> and in <italic>A. zonatus</italic>. UapA-like transporters are present outside the aspergilli (e.g. in <italic>N. crassa</italic> and in members of the Pezizales, a basal group of the Pezizomycotina), so the present data perhaps contradict the suggestion that UapC was the ancestral gene and UapA had arisen by a recent duplication [<xref ref-type="bibr" rid="CR207">207</xref>]. Second, UapD members were detected in section <italic>Nigri</italic>, but no data supporting their function as nucleobase transporters have yet been reported [<xref ref-type="bibr" rid="CR205">205</xref>]. Finally, the AzgA group comprises H<sup>+</sup> symporters specific for adenine, hypoxanthine, and guanine, and this group was present in all of the sequenced aspergilli [<xref ref-type="bibr" rid="CR204">204</xref>, <xref ref-type="bibr" rid="CR208">208</xref>, <xref ref-type="bibr" rid="CR209">209</xref>]. This family, despite no evident similarity in primary amino acid sequence, seems ancestrally related to the NAT family [<xref ref-type="bibr" rid="CR209">209</xref>].</p></sec><sec id="FPar2"><title>Nucleobase Cation Symport 1 family</title><p>Nucleobase Cation Symport 1 (NCS1) family (2.A.39) [<xref ref-type="bibr" rid="CR140">140</xref>] proteins are H<sup>+</sup> (or Na<sup>+</sup> in some bacteria) symporters specific for the uptake of purines, pyrimidines, thiamine, hydantoin, pyridoxine, and related metabolites in prokaryotes, fungi, and some plants. All members contain 12 TMDs and extended cytoplasmic tails. NCS1 transporters of the aspergilli and other dikarya can be divided into two distinct subfamilies, Fur and Fcy, both of which are probably the result of independent horizontal transfers from prokaryotes [<xref ref-type="bibr" rid="CR207">207</xref>]. Fur homologs in the aspergilli and penicillia have presviously been shown to exhibit patterns of gene loss and duplication [<xref ref-type="bibr" rid="CR195">195</xref>]. Homologs of FurD (uracil) and FurA (allantoin) were the only ones found to be present in all analyzed species in the present study. Convergent evolution has occurred within the Fur family several times, so that prediction of substrate specificities without functional assays is impossible [<xref ref-type="bibr" rid="CR195">195</xref>]. The phylogenetic relations of these transporters are shown in Additional file <xref rid="MOESM26" ref-type="media">26</xref>.</p><p>The Fcy family of <italic>A. nidulans</italic> includes an H<sup>+</sup>/cytosine-purine symporter (FcyB) [<xref ref-type="bibr" rid="CR210">210</xref>, <xref ref-type="bibr" rid="CR211">211</xref>] and recently identified cryptic transporters for either adenine or guanine [<xref ref-type="bibr" rid="CR212">212</xref>]. Orthologs and paralogs of Fcy were found to be present in most of the examined aspergilli and penicillia (Additional file <xref rid="MOESM27" ref-type="media">27</xref>).</p></sec></sec><sec id="Sec29"><title>Concentrative Nucleoside Transporters family</title><p>The Concentrative Nucleoside Transporters (CNT) family (2.A.41) [<xref ref-type="bibr" rid="CR140">140</xref>] is exemplified by CntA of <italic>A. nidulans</italic>, which functions as a general H<sup>+</sup>/nucleoside symporter [<xref ref-type="bibr" rid="CR195">195</xref>]. One Cnt-like homolog is present in most of the genomes investigated, with the homologs being extremely well conserved and fully syntenic, with variations only in the N-tail. However, they are not present in <italic>A. zonatus</italic> and <italic>A. aculeatus</italic>, but some evidence for remnants (pseudogenes) was observed. No homologs were found in <italic>S. pombe</italic>, <italic>S. cerevisiae</italic>, plants, protozoa, and archaea. The presence of an ortholog of CntA in <italic>C. albicans</italic> [<xref ref-type="bibr" rid="CR213">213</xref>] indicates a possible conservation of function throughout the Ascomycotina.</p></sec></sec><sec id="Sec30"><title>Flavohemoglobins and nitric oxide (NO) sensitivity</title><p>Nitric oxide (NO) is a gaseous radical with a short half-life and a high reactivity. For these reasons, fungi have evolved a diverse set of strategies to cope with NO [<xref ref-type="bibr" rid="CR214">214</xref>]. Flavohemoglobins are a family of conserved proteins in bacteria and fungi which have the ability to detoxify NO via an NADPH, FAD, and O<sub>2</sub>-dependent conversion of NO to NO<sub>3</sub><sup>–</sup> [<xref ref-type="bibr" rid="CR215">215</xref>]. Flavohemoglobins have been previously characterized in <italic>A. nidulans</italic> and <italic>A. oryzae</italic>, where two proteins have been identified [<xref ref-type="bibr" rid="CR216">216</xref>–<xref ref-type="bibr" rid="CR218">218</xref>]. In <italic>A. nidulans</italic>, it was found that deletion of both flavohemoglobins <italic>fhbA</italic> and <italic>fhb</italic>B resulted in increased sensitivity to NO [<xref ref-type="bibr" rid="CR216">216</xref>, <xref ref-type="bibr" rid="CR219">219</xref>]. In <italic>A. oryzae</italic>, FhbA was localized in the cytosol, while FhbB showed mitochondrial localization [<xref ref-type="bibr" rid="CR218">218</xref>], although it was also found that FhbA contains a predicted motif for secretion in <italic>A. niger</italic> and some other aspergilli [<xref ref-type="bibr" rid="CR217">217</xref>]. The cytosolic flavohemoglobin (<italic>fhbA</italic>) is regulated by nitrogen source and the mitochondrial one during development [<xref ref-type="bibr" rid="CR216">216</xref>, <xref ref-type="bibr" rid="CR219">219</xref>]. A cytochrome P450 nor (nitric oxide reductase) that reduces NO to N<sub>2</sub>O was found in <italic>Fusarium oxysporum</italic> [<xref ref-type="bibr" rid="CR220">220</xref>]. This P450nor is not widespread in aspergilli, being present only in six species (Fig. <xref rid="Fig11" ref-type="fig">11</xref>). A S-nitrosoglutathione (GSNO) reductase converts GSNO into ammonia and oxidized glutathione (GSSG) in <italic>Cryptococcus neoformans</italic> and <italic>Magnaporthe oryzae</italic> [<xref ref-type="bibr" rid="CR221">221</xref>, <xref ref-type="bibr" rid="CR222">222</xref>]. GSNO red is present in all <italic>Aspergillus</italic> species sequenced in this work. Some of the strains have up to three copies of this gene (Fig. <xref rid="Fig11" ref-type="fig">11</xref>).<fig id="Fig11"><label>Fig. 11</label><caption><p>Inhibition of growth by NO. The <italic>table</italic> depicts the number of homologs of the flavohaemoglobin genes (<italic>fhbA</italic> and <italic>fhbB</italic>), the P450 nitric oxide reductase, and the S-nitrosoglutathione (GSNO) reductase in each species. Strains are listed in the same order as in the phylogenetic tree shown in Fig. <xref rid="Fig1" ref-type="fig">1</xref>. Strains were grown in the presence or in the absence of the NO-releasing compound nitroprusside. Growth was monitored at different time intervals. The <italic>graph</italic> shows the percentage of growth in the presence of 128 mM nitroprusside compared to the control samples grown in the absence of nitroprusside. The time and temperature of growth was optimized for each strain and it was as follows (species name, strain, temperature, and incubation time for growth inhibition calculation): <italic>A. glaucus:</italic> 22 °C for 72 h; <italic>A. tubingensis</italic>: 30 °C for 96 h; <italic>A. zonatus</italic>: 30 °C for 96 h; <italic>A. brasiliensis</italic>: 30 °C for 72 h; <italic>A. versicolor</italic>: 30 °C for 96 h; <italic>A. sydowii</italic>: 30 °C for 96 h; <italic>A. niger</italic> ATCC1015: 30 °C for 48 h; <italic>A. luchuensis</italic>: 30 °C for 72 h; <italic>A. niger</italic> NRRL3: 30 °C for 72 h; <italic>A. wentii</italic>: 30 °C for 96 h; <italic>A. niger</italic> CBS 513.88: 30 °C for 96 h; <italic>A. fischeri</italic>: 30 °C for 96 h; <italic>A. terreus</italic>: 30 °C for 96 h; <italic>A. flavus</italic>: 30 °C for 96 h; <italic>A. fumigatus</italic>: 30 °C for 96 h; <italic>A. clavatus</italic>: 30 °C for 96 h; <italic>A. nidulans</italic>: 30 °C for 96 h; <italic>A. carbonarius</italic>: 30 °C for 72 h; <italic>A. aculeatus</italic>: 30 °C for 96 h</p></caption><graphic xlink:href="13059_2017_1151_Fig11_HTML" id="MO14"></graphic></fig></p><sec id="Sec31"><title>In silico analysis of flavohemoglobins</title><p>A search for homologs of flavohemoglobins in the genomes of the test aspergilli revealed that all these species contain at least one gene encoding flavohemoglobin A (Additional file <xref rid="MOESM28" ref-type="media">28</xref>). Five species contain two copies of flavohemoglobin A and eight species contain one <italic>fhbA</italic> and one <italic>fhbB</italic> in their genomes. Phylogenetic analysis confirmed that flavohemoglobins A and B form two well-defined clusters (data not shown). The duplication of flavohemoglobin A could have happened after the separation of the <italic>A. nidulans–A. versicolor–A. sydowii</italic> cluster, which groups separately from the rest of the aspergilli <italic>fhbA</italic> genes. Interestingly, the <italic>fhbB</italic> genes of these three species also cluster together.</p></sec><sec id="Sec32"><title>NO sensitivity</title><p>Most of the <italic>Aspergillus</italic> species were sensitive to high concentrations of the NO-releasing compound sodium nitroprusside (Fig. <xref rid="Fig11" ref-type="fig">11</xref>, Additional files <xref rid="MOESM3" ref-type="media">3</xref> and <xref rid="MOESM28" ref-type="media">28</xref>). However, some were resistant to NO, in particular <italic>A. glaucus</italic>, <italic>A. niger</italic> (NRRL3 and ATCC1015), and <italic>A. luchuensis.</italic> Other strains, such as <italic>A. tubingensis</italic> and <italic>A. carbonarius</italic>, showed an intermediate sensitivity to NO. We could not find any correlation between the sensitivity to NO displayed in our growth tests and the number of copies or the type of genes involved in the detoxification of NO. The presence of one or two types of flavohemoglobins (cytosolic or mitochondrial) and the fact that all species having two copies of <italic>fhbA</italic> do not have the other flavohemoglobin (<italic>fhbB</italic>) is intriguing. Although no association between number and/or type of flavohemoglobin and sensitivity to NO is evident, it may reflect an adaptation to different lifestyles. However, all species contain three to six copies of NO detoxification genes with at least two types of mechanisms (Fig. <xref rid="Fig11" ref-type="fig">11</xref>). For example, in <italic>A. fumigatus</italic> detoxification of NO does not seem to be required for full virulence [<xref ref-type="bibr" rid="CR223">223</xref>, <xref ref-type="bibr" rid="CR224">224</xref>] and it contains only three genes for the NO detoxification (two flavohemoglobins and one GSNO reductase) (Fig. <xref rid="Fig11" ref-type="fig">11</xref>).</p></sec></sec><sec id="Sec33"><title>Signal transduction pathway genes</title><p>Gene family members for four different protein classes involved in signal transduction in Eurotiomycetes were identified using a protein domain-based approach. In total 11,120 proteins were identified belonging to 29 Eurotiomycetes species, clustered into 765 orthologous groups. The analysis of orthologous groups produced a set of genes that could not be clustered with any other and are regarded here as putative species-specific genes. Of the 29 Eurotiomycetes genomes, 25 contain species-specific genes (Fig. <xref rid="Fig12" ref-type="fig">12a</xref>) that may be involved in particular traits of these species. G-protein-coupled receptor (GPCRs) and kinases contribute most to these genomic novelties and thus constitute candidates for further functional studies aiming at understanding the differences among them (Additional file <xref rid="MOESM29" ref-type="media">29</xref>).<fig id="Fig12"><label>Fig. 12</label><caption><p><bold>a</bold> Proportion of species-specific genes of the different signal transduction protein-classes in Eurotiomycetes. <bold>b</bold> Number of protein phosphatases in fungi. Eurotiomycetes appear in <italic>red</italic></p></caption><graphic xlink:href="13059_2017_1151_Fig12_HTML" id="MO15"></graphic></fig></p><sec id="Sec34"><title>G-protein receptors and subunits</title><p>Heterotrimeric G-proteins have universal roles as signaling proteins in eukaryotes. Each G-protein heterotrimer is composed of α, β, and γ subunits that interact with the plasma-membrane, in association with a GPCR. Most filamentous fungi have three conserved Gα subunits (I, II, and III), one Gβ protein, and one Gγ protein. The number of predicted GPCRs varies widely, with a larger number identified in ascomycete than in basidiomycete fungi [<xref ref-type="bibr" rid="CR225">225</xref>–<xref ref-type="bibr" rid="CR227">227</xref>]. Results of the domain-based identification of G-proteins and GPCR orthologs in the eurotiomycetes are illustrated in Additional file <xref rid="MOESM28" ref-type="media">28</xref>. Gα proteins were found to be highly conserved. The Gα group I (<italic>fadA</italic>) regulates multiple pathways; most filamentous fungi in this study have a single copy of this gene (Additional files <xref rid="MOESM29" ref-type="media">29</xref> and <xref rid="MOESM30" ref-type="media">30</xref>). In contrast, Group II Gα proteins (<italic>ganA</italic>) are less conserved than the other Gα proteins and up to three copies were found in one species (<italic>T. stipitatus</italic>) (Additional file <xref rid="MOESM30" ref-type="media">30</xref>). The Group II Gα proteins play a positive role in germination of conidia, possibly through cAMP signaling in carbon sensing [<xref ref-type="bibr" rid="CR228">228</xref>, <xref ref-type="bibr" rid="CR229">229</xref>]. The last Gα belongs to group III (<italic>ganB</italic>) and was found as a single copy in all eurotiomycetes where it is thought to act as a negative regulator (Additional files <xref rid="MOESM2" ref-type="media">2</xref>, <xref rid="MOESM29" ref-type="media">29</xref>, and <xref rid="MOESM30" ref-type="media">30</xref>). Additionally, we found three different Gα groups of orthologs (Clusters FungiJGICTBE21135 only present in <italic>A. niger</italic> ATCC 1015, FungiJGICTBE20122 present in <italic>A. flavus</italic> NRRL 3557 and in <italic>A. oryzae</italic> RIB40, and FungiJGICTBE14195 present in <italic>A. flavus</italic> NRRL 3557 (Additional files <xref rid="MOESM29" ref-type="media">29</xref> and <xref rid="MOESM30" ref-type="media">30</xref>) that appear to be encode genes that contain the Gα domain. There was also one copy of the Gβ negative regulator of asexual reproduction (<italic>sfaD</italic>) in each genome (Additional files <xref rid="MOESM2" ref-type="media">2</xref>, <xref rid="MOESM30" ref-type="media">30</xref>, and <xref rid="MOESM31" ref-type="media">31</xref>) [<xref ref-type="bibr" rid="CR230">230</xref>]. Finally, all Eurotiomycetes genomes contained a single highly conserved Gγ gene [<xref ref-type="bibr" rid="CR231">231</xref>].</p></sec><sec id="Sec35"><title>Serine-arginine protein kinases</title><p>Members of the serine-arginine protein kinases (SRPKs) family are known to phosphorylate serine within RS (arginine/serine rich) regions [<xref ref-type="bibr" rid="CR232">232</xref>]. As previously reported in <italic>A. nidulans</italic>, <italic>N. crassa</italic>, and dermatophytes, there is high genome expansion of SRPKs in filamentous fungi [<xref ref-type="bibr" rid="CR21">21</xref>]. Interestingly, the <italic>A. nidulans</italic> SRPK types were spread in seven clusters of orthologous genes, whereas only two SRPK types have been found in <italic>N. crassa</italic> (Additional file <xref rid="MOESM32" ref-type="media">32</xref>). However, <italic>A. nidulans</italic> is the only eurotiomycete with all seven SRPK types. Most of the SRPK members identified in Eurotiomycetes belong to the types A and F, while the SrpkB and SrpkD types were less conserved in the eurotiomycete genomes. It has been suggested that SRPKs of filamentous fungi are involved in the molecular response to a broad range of environmental stimuli, although these signaling pathways are currently poorly understood [<xref ref-type="bibr" rid="CR233">233</xref>]. Since the main biological role for SRPKs is the regulation of messenger RNA (mRNA) processing, it is conceivable to speculate that the expansion of SRPK in the eurotiomycetes could reflect the greater importance of splicing in filamentous fungi than in <italic>S. cerevisiae</italic>, whose genes generally do not contain introns. A core set of 48 kinases is present in all eurotiomycetes and in other species of Ascomycota analyzed (<italic>N. crassa</italic>, <italic>F. oxysporum</italic>, <italic>T. reesei</italic>, <italic>S. cerevisiae</italic>, <italic>P. pastoris</italic>, and <italic>S. pombe</italic>), which suggests that these kinases have a critical role in the biology of those organisms. Components of mitogen-activated protein (MAP) kinases are classical examples of conserved kinases [<xref ref-type="bibr" rid="CR234">234</xref>] and are involved in cell polarity and cell wall maintenance (Kin1, BckA, MkkA, MpkA), mating (SteC, Ste7, Ste 20), and osmotic stress sense (HogA, SskB, PbsA) [<xref ref-type="bibr" rid="CR233">233</xref>].</p><p>In contrast to the above conserved pathways, there is growing evidence that filamentous fungi might have evolved unique kinases. Indeed, a block of kinases that appear to be specific to filamentous fungi have been identfied, named filamentous fungal kinases (Ffk from A to J). These show low sequence identity with kinases of <italic>S. cerevisiae</italic>, <italic>Caenorhabditis elegans</italic>, <italic>Drosophila melanogaster</italic>, and human [<xref ref-type="bibr" rid="CR233">233</xref>].</p><p>Since single deletions of FfkA, FfkB, FfkD, FfkE, FfkF, FfkG, FfkH, and FfkI from <italic>A. nidulans</italic> were not lethal and did not give a different phenotype [<xref ref-type="bibr" rid="CR233">233</xref>], little is known about the functionality of these kinases [<xref ref-type="bibr" rid="CR99">99</xref>]. The present study found a similar group of kinases among the Eurotiomycetes that do not appear to have orthologs in the yeast species analyzed (Table <xref rid="Tab6" ref-type="table">6</xref>) [<xref ref-type="bibr" rid="CR233">233</xref>]. Overall, <italic>P. pastoris</italic>, <italic>S. cerevisiae</italic>, and <italic>S. pombe</italic> encode fewer kinase orthologs than the other fungal species analyzed, with 98, 126, and 101 copies, respectively, which is almost half the number of kinases predicted in the <italic>P. rubens</italic> Wisconsin (205). Conversely, there is a core set of 31 kinases (Additional file <xref rid="MOESM33" ref-type="media">33</xref>) that do not appear in any of the eurotiomycetes, but were retained in <italic>S. cerevisiae</italic>, <italic>P. pastoris</italic>, and/or <italic>S pombe</italic>. Twenty-five kinases are essential in <italic>A. nidulans</italic> [<xref ref-type="bibr" rid="CR233">233</xref>] and all the analyzed eurotiomycetes have at least one copy of these genes, suggesting they are essential across the tested species.<table-wrap id="Tab6"><label>Table 6</label><caption><p>Filamentous fungal kinases without orthologs in model yeast species</p></caption><table frame="hsides" rules="groups"><thead><tr><th>Cluster</th><th><italic>A. nidulans</italic> kinase locus tag</th><th>Domain</th><th><italic>A. nidulans</italic> name</th><th>Picpa1</th><th>Sacce1</th><th>SacceM3707_1</th><th>Schpo1</th></tr></thead><tbody><tr><td>FungiJGICTBE4492</td><td>AN10485</td><td>Pkinase</td><td>Stk21</td><td>0</td><td>0</td><td>0</td><td>0</td></tr><tr><td>FungiJGICTBE1792</td><td>AN6339</td><td>Pkinase</td><td>Pod6</td><td>0</td><td>0</td><td>0</td><td>0</td></tr><tr><td>FungiJGICTBE4614</td><td>AN1560</td><td>Pkinase</td><td>PlkA</td><td>0</td><td>0</td><td>0</td><td>0</td></tr><tr><td>FungiJGICTBE4599</td><td>AN4717</td><td>Pkinase</td><td>PkaB</td><td>0</td><td>0</td><td>0</td><td>0</td></tr><tr><td>FungiJGICTBE3865</td><td>AN0822</td><td>Pkinase</td><td>KfsA</td><td>0</td><td>0</td><td>0</td><td>0</td></tr><tr><td>FungiJGICTBE1403</td><td>AN4936</td><td>Pkinase</td><td>Prp4</td><td>0</td><td>0</td><td>0</td><td>1</td></tr><tr><td>FungiJGICTBE4249</td><td>AN7537</td><td>Pkinase</td><td>Ppk33</td><td>0</td><td>0</td><td>0</td><td>1</td></tr><tr><td>FungiJGICTBE2868</td><td>AN3101</td><td>HiskA</td><td>PhkB</td><td>0</td><td>0</td><td>0</td><td>1</td></tr><tr><td>FungiJGICTBE1795</td><td>AN3102</td><td>HisKA</td><td>PhkA</td><td>0</td><td>0</td><td>0</td><td>2</td></tr><tr><td>FungiJGICTBE4245</td><td>AN6044</td><td>Pkinase</td><td>NpkA</td><td>0</td><td>0</td><td>0</td><td>1</td></tr><tr><td>FungiJGICTBE4202</td><td>AN3065</td><td>Pkinase</td><td>CmkB</td><td>0</td><td>0</td><td>0</td><td>1</td></tr><tr><td>FungiJGICTBE3486</td><td>AN0699</td><td>Pkinase</td><td>Cak1</td><td>0</td><td>0</td><td>0</td><td>1</td></tr><tr><td>FungiJGICTBE668</td><td>AN4479</td><td>HisKA</td><td>NikA</td><td>2</td><td>0</td><td>0</td><td>0</td></tr><tr><td>FungiJGICTBE164</td><td>AN11032</td><td>Pkinase</td><td>SepL</td><td>1</td><td>0</td><td>0</td><td>1</td></tr><tr><td>FungiJGICTBE3739</td><td>AN4385</td><td>Pkinase</td><td>SepH</td><td>1</td><td>0</td><td>0</td><td>1</td></tr><tr><td>FungiJGICTBE3573</td><td>AN10800</td><td>BCDHK_Adom3</td><td>pkpA</td><td>1</td><td>0</td><td>0</td><td>1</td></tr><tr><td>FungiJGICTBE2991</td><td>AN11101</td><td>Pkinase</td><td>Gin4</td><td>1</td><td>0</td><td>0</td><td>1</td></tr><tr><td>FungiJGICTBE3299</td><td>AN5728</td><td>Pkinase</td><td>Stk22</td><td>0</td><td>1</td><td>1</td><td>1</td></tr><tr><td>FungiJGICTBE2936</td><td>AN10515</td><td>Pkinase</td><td>PrK1</td><td>0</td><td>1</td><td>1</td><td>1</td></tr><tr><td>FungiJGICTBE598</td><td>AN1665</td><td>Pkinase</td><td>stk51</td><td>1</td><td>1</td><td>1</td><td>0</td></tr><tr><td>FungiJGICTBE878</td><td>AN2412</td><td>Pkinase</td><td>CmkA</td><td>1</td><td>2</td><td>2</td><td>0</td></tr><tr><td>FungiJGICTBE3318</td><td>AN7563</td><td>Pkinase</td><td>ChkC</td><td>1</td><td>1</td><td>1</td><td>0</td></tr></tbody></table></table-wrap></p></sec><sec id="Sec36"><title>Protein phosphatases</title><p>Protein phosphatases are classified into the following main groups: (1) classical Ser/Thr phosphatases: phosphoprotein phosphatases (PPP) family and protein phosphatase Mg<sup>2+</sup> or Mn<sup>2+</sup> dependent (PPM) family; (2) protein Tyr phosphatase (PTP superfamily); and (3) Asp-based protein phosphatases with DXDXT/V catalytic signature (CPDs) [<xref ref-type="bibr" rid="CR235">235</xref>]. Ssu72, a different type of protein phosphatases, is regarded as separate, although it shares some similarity with the PTP Superfamily [<xref ref-type="bibr" rid="CR236">236</xref>]. We found, on average, 8.8 PPPs, 8.37 PPMs, 5.26 CPDs, and 15.3 PTPs in the fungi included in this study (Fig. <xref rid="Fig12" ref-type="fig">12b</xref>). The actual numbers varied considerably between species, especially for the PTPs. Ssu72, is an exception, showing a single member in all species. PTP is the largest phosphatase superfamily presented here, including classical PTPs [<xref ref-type="bibr" rid="CR236">236</xref>], dual-specificity phosphatases (DSPases), that have an important role in intracellular transduction pathways and regulate the mitogen-activated protein kinase (MAPK) pathway and cell cycle progression, Cdc25 type phosphatases, either regulating cell cycle progression [<xref ref-type="bibr" rid="CR237">237</xref>], and low molecular weight phosphatases [<xref ref-type="bibr" rid="CR236">236</xref>]. The increased and variable repertoire of protein kinases and phosphatases in <italic>Aspergillus</italic> could have helped in the establishment of several complex morphological traits, as well, as sophisticated responses to stress and the evolution of pathways that can help in the pathogenic process.</p></sec></sec><sec id="Sec37"><title>DNA protein organisation and methylation</title><sec id="Sec38"><title>Histones of the aspergilli</title><p>Five classes of histones have been identified in eukaryotes, comprising linker histone H1 and core histones H2A, H2B, H3, and H4. Bioinformatic analysis of the newly available <italic>Aspergillus</italic> genome sequences revealed the presence of all of these families of histones, with overall evidence of conservation throughout the aspergilli. However, there were some differences between species, the functional implications of which are unclear, as follows.</p><p>All analyzed <italic>Aspergillus</italic> genomes were found to contain an H1 histone gene, following manual curation. The sequences are highly similar at the N-terminus and within the globular domain (residues 18–93 in <italic>A. nidulans</italic>, Additional file <xref rid="MOESM34" ref-type="media">34</xref>). They diverge in the C-terminal domain, the maximal divergence being at the boundary of the globular domain with the C-terminal domain, due mainly to sequence insertions.</p><p>All <italic>Aspergillus</italic> genomes also contain a highly conserved H2B histone.</p><p>As previously reported [<xref ref-type="bibr" rid="CR238">238</xref>], in the aspergilli, as in other ascomycetes, the extant H2A histone corresponds to the H2AX variant, rather than the canonical H2A form. This was confirmed for all aspergilli in the databases, where the diagnostic motif SQEL is conserved at the carboxy terminus. In all aspergilli, as reported previously for <italic>A. nidulans</italic> and <italic>N. crassa</italic> [<xref ref-type="bibr" rid="CR239">239</xref>, <xref ref-type="bibr" rid="CR240">240</xref>], the H2AX gene is transcribed divergently from the H2B gene. In addition, all analyzed <italic>Aspergillu</italic>s genomes have an H2A.Z ortholog. While nothing is known about the role of this histone in any of the Pezizomycotina, the cognate gene is not essential in <italic>N. crassa</italic>, <italic>S. cerevisiae</italic>, or <italic>S. pombe</italic> [<xref ref-type="bibr" rid="CR241">241</xref>, <xref ref-type="bibr" rid="CR242">242</xref>]<italic>.</italic></p><p>All analyzed genomes contain an H3 gene, with complete amino acid sequence conservation for all species. While we have previously reported the presence of genes with significant amino acid similarity with histone H3 in <italic>A. terreus</italic> and <italic>A. oryzae</italic> [<xref ref-type="bibr" rid="CR238">238</xref>], no other H3 paralogs were found in the other aspergilli nor in any of the other eurotiomycete genomes. The paralog in <italic>A. terreus</italic> appears real with two typical filamentous fungal introns but we could not find evidence for its expression in publicly available data. In the six sequenced strains of <italic>A. oryzae</italic>, as well as in the genome of the strongly related species <italic>A. sojae</italic> and <italic>A. parasiticus</italic> [<xref ref-type="bibr" rid="CR243">243</xref>–<xref ref-type="bibr" rid="CR245">245</xref>], a duplication has occurred of the central part of the functional H3 gene but no legitimate start-codon could be identified. There is no similarity among these sequences downstream of the H3-like sequence [<xref ref-type="bibr" rid="CR238">238</xref>], which suggests that this “gene” results from a non-functional duplication of part of the canonical H3-encoding gene. This duplication is, however, absent in the ten currently sequenced strains of <italic>A. flavus</italic> [<xref ref-type="bibr" rid="CR246">246</xref>]. The occurrence of a genetic feature common <italic>to A. sojae</italic>, <italic>A. parasiticus</italic>, and <italic>A. oryzae</italic> but absent from <italic>A. flavus</italic> (and <italic>A. nomius</italic>) is intriguing given the fact that <italic>A. oryzae</italic> are generally considered domesticated variants of <italic>A. flavus</italic> [<xref ref-type="bibr" rid="CR9">9</xref>].</p><p>All species also contain the specific centromeric H3 histone (naming varies in different organisms, here named CenH3), with the motif LPFAR in helix α1 conserved in all species. Alignment of the CenH3 sequences (Additional file <xref rid="MOESM34" ref-type="media">34</xref>) shows the typical CenH3 divergence in the N-terminal region, which is a highly variable region in different species of <italic>D. melanogaster</italic> [<xref ref-type="bibr" rid="CR247">247</xref>], confirming previous observations [<xref ref-type="bibr" rid="CR238">238</xref>]. Additional file <xref rid="MOESM34" ref-type="media">34</xref> also shows comparative phylogenies of the CenH3 histone and of the other sequence-variable histone, H1. CenH3 histone divergence has been proposed to be instrumental in driving speciation [<xref ref-type="bibr" rid="CR247">247</xref>].</p><p>All genomes have two H4 encoding genes, one transcribed divergently from the H3 encoding gene, denoted H4.I, and a second one, denoted H4.II, unlinked to it. The H3-linked and unlinked H4 paralogs are almost identical at the amino acid sequence but the intron organization of the paralogs differs. Both H4 genes share an intron that splits the Arg4 codon. In H4.II, this is the only intron (in <italic>Aspergillus</italic> and <italic>Penicillium</italic>) and it is always at least twice as big as that in the H4.I paralog, often >200–350 nt. The H4.I gene generally has a second intron interrupting the Arg96 codon. This 3′ intron must have been lost in <italic>A. zonatus</italic>, <italic>A. glaucus</italic>, <italic>A. rubrum</italic>, and also in <italic>Penicillium paxilli</italic>, since it is present in the eight sequenced species that belong to other families of Eurotiales (<italic>Talaromyces</italic>, <italic>Thermoascus</italic>, <italic>Monascus</italic>, <italic>Byssochlamys</italic>, and <italic>Thermomyces</italic>) and in Onygenales. In addition, the amino acid at position 2 is a Ser or Thr in both I and II paralogs. Note that in a given species, paralogs I and II are always identical at this position (Ser for <italic>A. flavus</italic>, <italic>A. glaucus</italic>, <italic>A. nidulans</italic>, <italic>A. oryzae</italic>, and <italic>A. sydowii</italic> and <italic>A. versicolor</italic>, <italic>A. rubrum</italic>, and Thr for the other sequenced aspergilli). These species belong to different taxonomic sections within the aspergilli, suggesting that concerted evolution (possibly by gene conversion) could be responsible for the residue at this position. Similarly, at position 65, there is almost always a Thr in paralog I, which is a Ser in paralog II. At position 69, there is always a Gly in paralog I and a Ser in paralog II.</p><p>We have reported previously the presence of a small reading frame with significant similarity to a central part of histone H4 in the genome of <italic>A. nidulans</italic> [<xref ref-type="bibr" rid="CR238">238</xref>]. We have now found similar reading frames in most <italic>Aspergillus</italic> genomes. This include species where it was previously overlooked or where it was erroneously annotated. The newly recognized “third” histone 4 gene invariably contains seven introns. As a consequence, this gene has considerably more intronic sequences than coding sequences; in <italic>A. nidulans</italic> for instance, the 357 nt long coding sequence (36%) is interrupted by 642 nt of intronic sequences (64%). The additional putative H4 gene is absent from <italic>A. glaucus</italic> and <italic>E. rubrum</italic> as well as from <italic>Penicillium</italic> species, but present in other sequenced Eurotiales species as well as in the Onygenales (Additional file <xref rid="MOESM34" ref-type="media">34</xref>).</p></sec><sec id="Sec39"><title>Putative DNA methylases</title><p>Two putative DNA methylases have been described in the ascomycetes. They were identified through work relating to the phenomena of MIP (Masc1, <italic>Ascobolus immersus</italic>) and RIP (RID1, <italic>N. crassa</italic>) as inactivation of the <italic>masc1</italic> and <italic>rid‐1</italic> prevent MIP and RIP, respectively [<xref ref-type="bibr" rid="CR248">248</xref>, <xref ref-type="bibr" rid="CR249">249</xref>].</p><p>There are, however, serious doubts as to whether <italic>masc1</italic> and <italic>rid-1</italic> encode actual DNA methylases. First, no DNA methylase activity could be detected in vitro with the purified proteins [<xref ref-type="bibr" rid="CR248">248</xref>, <xref ref-type="bibr" rid="CR249">249</xref>]. Second, all DNA methylation in <italic>N. crassa</italic>, even methylation subsequent to RIP, depends on another protein, DIM2 [<xref ref-type="bibr" rid="CR250">250</xref>]. Third, a homolog of Masc1 and RID1 was reported for <italic>A. nidulans</italic> (DmtA), a species for which DNA methylation has never been detected [<xref ref-type="bibr" rid="CR251">251</xref>, <xref ref-type="bibr" rid="CR252">252</xref>] (Reyes Domínguez and Scazzocchio, unpublished data). Similar results were obtained for <italic>A. flavus</italic> [<xref ref-type="bibr" rid="CR253">253</xref>]. Interestingly, DmtA is essential for meiosis in <italic>A. nidulans</italic> [<xref ref-type="bibr" rid="CR251">251</xref>].</p><p>All the sequenced aspergilli were found to have Masc1/RID1 homologs at syntenic positions. A phylogentic tree shows DIM2 as outgroup to all other sequences (Additional file <xref rid="MOESM35" ref-type="media">35</xref>), while RID1 of <italic>N. crassa</italic> clusters with the two <italic>Talaromyces</italic> species, which, in the absence of other sequences in the tree, may simply mean that the latter have diverged less from an ancestral homolog. The pervasive presence of the DmtA orthologs may indicate that many <italic>Aspergillus</italic> and <italic>Penicillium</italic> “asexual” species are in fact sexual (see earlier “<xref rid="Sec4" ref-type="sec">Asexual and sexual reproduction</xref>” section).</p><p>A DNA methylase with in vitro enzyme activity, Masc2, has been described in <italic>A. immersus</italic> [<xref ref-type="bibr" rid="CR254">254</xref>] and BLAST analysis revealed a new protein family present in all aspergilli in syntenic positions. The <italic>A. nidulans</italic> protein includes from residue 322 to 586 a putative (incomplete) C‐5 cytosine DNA methylase domain while two (incomplete) SNF_2N domains occur from residues 1305 to 1470 and 1627 to 1818. No function is known for this protein or its homologs, but orthologs are present in all available sequences of <italic>Penicillium</italic> and <italic>Talaromyces</italic>, and in <italic>A. immersus</italic> and <italic>Tuber melanosporum</italic>, members of Pezizales, a basal order of the Pezizomycotina. Interestingly, in <italic>N. crassa</italic>, the fungus where DNA methylation has been more thoroughly studied, no protein with the same architecture is present nor was one found in most other Sordariomycetes.</p></sec></sec></sec><sec id="Sec40"><title>Conclusions</title><p>Data presented in the present study emphasize the high genomic and functional diversity present within the genus <italic>Aspergillus</italic>. While strong conservation was observed for central biological functions (e.g. sporulation, aspects of cell wall structure, and histones), high diversity was apparent for many other physiological traits, such as carbon utilization, secondary metabolism, and stress response. While most aspergilli can occupy a broad range of habitats, our data suggest that evolution has generated considerable diversity within the genus to allow their exploitation of and persistence in different habitats.</p><p>The detailed analyses described in this paper will serve as a reference for variation in other fungal species. The unique position of this genus in the genomics of filamentous fungi, with genome sequences for a large number of species, will become even more evident with the future completion of the currently ongoing <italic>Aspergillus</italic> whole genus genome project in which more than 300 genomes from species of this genus will be sequenced. The data of our study will provide a backbone to rapidly perform detailed genomic comparisons and functional studies in these new genomes.</p></sec><sec id="Sec41"><title>Methods</title><sec id="Sec42"><title>Genome sequencing, assembly, and annotation</title><sec id="Sec43"><title>Genome sequencing and assembly</title><p>The majority of genomes and transcriptomes in this study (<italic>A. luchuensis</italic>, <italic>A. brasiliensis</italic>, <italic>A. glaucus</italic>, <italic>A. sydowii</italic>, <italic>A. tubingensis</italic>, <italic>A. wentii</italic>, <italic>A. versicolor</italic>, and <italic>A. zonatus</italic>,) were sequenced with Illumina and assembled with AllPathsLG [<xref ref-type="bibr" rid="CR255">255</xref>], except for <italic>A. aculeatus</italic> and <italic>A. carbonarius</italic>, which were sequenced using a combination of 454 and Sanger platforms and assembled with Newbler (Roche). For all standard fragment Illumina libraries, 500 ng–1 μg of genomic DNA was sheared using the Covaris E210 (Covaris) and sized selected for 270 bp using Agencourt Ampure Beads (Beckman Coulter). The DNA fragments were treated with end repair, A-tailing, and adapter ligation using the TruSeq DNA Sample Prep Kit (Illumina) and purified using Agencourt Ampure Beads (Beckma Coulter). These were sequenced on HiSeq in 2 × 150 bp read format and assembled using AllPathsLG with long-mate paired-end libraries, which were built using several approaches.</p><p>CLIP (Cre-Lox Inverse PCR) libraries were used for all Illumina sequenced genomes in this study except for <italic>A. zonatus</italic> and <italic>A. glaucus</italic>. For CLIP libraries, 10–15 μg of genomic DNA were sheared using the Hydroshear® and gel size selected for 4–5 kb. The fragments were end-repaired (NEB) and ligated with biotinylated Illumina compatible adapters containing loxP (IDT). The adapter ligated DNA fragments were circularized via recombination by a Cre excision reaction (NEB). The circularized DNA was digested using four base cutter restriction enzymes followed by self-ligation (NEB). The self-ligated products were immobilized on beads and inverse PCR was used to enrich for the final library (NEB). For <italic>A. zonatus</italic> and <italic>A. glaucus</italic>, ligation-free paired-end (LFPE) fragments were used. LFPE fragments were generated using the 5500 SOLiD Mate-Paired Library Construction Kit (SOLiD®). A total of 15 μg of genomic DNA was sheared using the Covaris g-TUBETM (Covaris) and gel size selected for 5 kb. The sheared DNA was end-repaired and ligated with biotinylated internal linkers. The DNA was circularized using intra-molecular hybridization of the internal linkers. The circularized DNA was treated with plasmid safe to remove non-circularized products. The circularized DNA was nick translated and treated with T7 exonuclease and S1 nuclease to generate fragments containing internal linkers with genomic tags on each end. The mate pair fragments were A-tailed and purified using Strepavidin bead selection (Invitrogen). The purified fragments were ligated with Illumina adaptors and amplified using ten cycles of PCR with Illumina primers (Illumina) to generate the final library. Quantitative PCR (qPCR) was used to determine the concentration of the libraries and were sequenced on the Illumina Hiseq in format 2 × 100 bp reads.</p><p>All Illumina reads from both types of libraries for each genome were assembled using AllPathsLG.</p><p>The genomes of <italic>A. aculeatus</italic> and <italic>A. carbonarius</italic> were sequenced using a combination of 454 standard, 454 paired-end, and Sanger fosmid libraries and assembled with Newbler. For 454 standard libraries, genomic DNA was fragmented by nebulization and purified using Ampure beads (Beckman Coulter). The ends of the fragments were treated with end repair and ligated with biotinylated adapters using either the Titanium (for <italic>A. aculeatus</italic>) or GS FLX (for <italic>A. carbonarius</italic>) Library Prep Kits (454). Adapter ligated products were immobilized on beads and treated with nick repair. Single strands were eluted to generate the final library. For 454 paired-end libraries, genomic DNA was sheared to 10 kb (for <italic>A. aculeatus</italic>) and 3 kb (for <italic>A. carbonarius</italic>) using the Hydroshear®. The ends of the fragments were ligated with biotinylated adapters containing loxP. The adapter ligated DNA fragments were gel-size selected and circularized via recombination by a Cre excision reaction (NEB). The circularized DNA was randomly sheared using the Covaris E210 (Covaris). The sheared fragments were end-repaired (NEB), ligated with 454 adapters (Roche), and immobilized on strepavidin beads followed by PCR using a biotinylated primer (Roche). The PCR product was immobilized and single-strand DNA libraries were isolated using an alkaline treatment. Sanger fosmid libraries for <italic>A. aculeatus</italic> and <italic>A. carbonarius</italic> were prepared from 20 ug of genomic DNA, sheared using the Hydroshear® and size selected for 40 kb using a pulse field gel. The long inserts were cloned into pCC1FOS vector. The hybrid 454-Sanger assemblies were produced using Newbler (Roche).</p></sec><sec id="Sec44"><title>Transcriptome sequencing and assembly</title><p>For all transcriptomes in this study, except for <italic>A. aculeatus</italic> and <italic>A. carbonarius</italic>, stranded complementary DNA (cDNA) libraries were generated using the Illumina mRNA sample preparation kit (Illumina). mRNA was purified from 10 μg of total RNA using magnetic beads containing poly-T oligos. mRNA was fragmented using divalent cations and high temperature. The fragmented RNA was reverse transcribed using random hexamers and SSII (Invitrogen) followed by second strand synthesis. The fragmented cDNA was treated with end-pair, A-tailing, adapter ligation, and ten cycles of PCR. qPCR was used to determine the concentration of the libraries. Libraries were sequenced on the Illumina Hiseq in 2 × 100 bp read format. Illumina reads were de novo assembled into consensus sequences using Rnnotator (v. 2.5.2 or later) [<xref ref-type="bibr" rid="CR256">256</xref>]. For <italic>A. aculeatus</italic>, cDNA libraries were generated using the cDNA Rapid Library Preparation Kit (Roche). mRNA was purified from total RNA using Absolutely mRNA™ purification kit (Stragene) and chemically fragmented using high heat. The fragmented RNA was reversed transcribed using random hexamers and AMV RT followed by second strand synthesis. The cDNA fragments were treated with end repair and ligated with 454 adapters. For <italic>A. carbonarius</italic>, mRNA was purified from total RNA using Absolutely mRNA™ purification kit (Stratagene). mRNA was reverse transcribed with SuperScriptIII using dT15VN2 primer. cDNA was synthesized with <italic>E. coli</italic> DNA Ligase, <italic>E. coli</italic> DNA polymerase I, and <italic>E. coli</italic> RnaseH (Invitrogen). cDNA was nebulized and gel purified to generate fragment sizes between 500–800 bp. The fragments were end-repaired, adaptor ligated, and made into single-strand DNA libraries using the GS FLX Titanium library kit. In both cases, 454 reads were filtered and screened for quality and contamination to include removal of ribosomal RNA, low-quality, and low-complexity reads. The remaining reads were assembled into contigs using Newbler (v2.3-PreRelease-6/30/2009) with default parameters.</p></sec><sec id="Sec45"><title>Genome annotation</title><p>Genome assembly scaffolds were masked with RepeatMasker [<xref ref-type="bibr" rid="CR257">257</xref>], RepBase library repeats [<xref ref-type="bibr" rid="CR258">258</xref>], and repeats frequently detected (>150 times) by RepeatScout [<xref ref-type="bibr" rid="CR259">259</xref>]. A combination of gene predictors was run on the masked assemblies: ab initio Fgenesh [<xref ref-type="bibr" rid="CR260">260</xref>] and GeneMark [<xref ref-type="bibr" rid="CR261">261</xref>]; homology-based Fgenesh + [<xref ref-type="bibr" rid="CR260">260</xref>] and Genewise [<xref ref-type="bibr" rid="CR262">262</xref>] seeded by BLASTx [<xref ref-type="bibr" rid="CR263">263</xref>] alignments against the NCBI NR database; and transcriptome-based assemblies. In addition to protein-coding genes, tRNAs were predicted using tRNAscan-SE [<xref ref-type="bibr" rid="CR264">264</xref>]. Predicted proteins were functionally annotated using SignalP [<xref ref-type="bibr" rid="CR265">265</xref>] to predict signal peptides, TMHMM [<xref ref-type="bibr" rid="CR266">266</xref>] for transmembrane domains, InterProScan [<xref ref-type="bibr" rid="CR267">267</xref>] for protein domains, and protein alignments to NCBI NR, SwissProt, KEGG [<xref ref-type="bibr" rid="CR268">268</xref>] for metabolic pathways, and KOG [<xref ref-type="bibr" rid="CR269">269</xref>] for eukaryotic clusters of orthologs. Interpro and SwissProt hits were used to map Gene Ontology terms [<xref ref-type="bibr" rid="CR270">270</xref>]. For each genomic locus, the best representative gene model was selected based on a combination of protein homology and EST support, which resulted in the final set of models used in this work.</p></sec><sec id="Sec46"><title>Protein conservation and phylogeny</title><p>To assess protein conservation, we performed MCL clustering [<xref ref-type="bibr" rid="CR271">271</xref>] with an inflation parameter of 2.0 on the 400,447 protein sequences from 37 predicted full fungal proteomes (25 from the Aspergillaceae, 12 ascomycete outgroups). Some 65,450 protein clusters (or families) resulted, with average size 6.12 including singletons and 19.40 excluding singletons, largest cluster containing 2179 proteins, and 47,245 singletons. Membership in a cluster was used to determine whether a protein was conserved across the comparative organism set. We considered a protein conserved if its homologs were found at least once in all members of an organism subset (e.g. section <italic>Nigri</italic> or Aspergillaceae). A protein was considered specific to an organism subset if it was found in at least one organism of the subset, but not in any organisms outside the subset.</p><p>Pfam domains [<xref ref-type="bibr" rid="CR272">272</xref>] were assigned using v. 22 of the database and a TimeLogic Decypher machine and an e-value of 10<sup>–4</sup>.</p><p>The phylogenetic tree was generated from a separate cluster run which differed from the previous one by the addition of non-ascomycete outgroups <italic>Rhizopus oryzae</italic> and <italic>Batrachochytrium dendrobatidis</italic> (JGI portals Rhior3 and Batde5, respectively; omitted from Fig. <xref rid="Fig1" ref-type="fig">1</xref>). Protein sequences with single copies in each organism were aligned using MAFFT [<xref ref-type="bibr" rid="CR273">273</xref>], trimmed to well-aligned regions using Gblocks [<xref ref-type="bibr" rid="CR274">274</xref>] with default parameters. RAxML [<xref ref-type="bibr" rid="CR275">275</xref>] was then run using the PROTMIXWAG model and <italic>B. dendrobatidis</italic> set as an outgroup to generate the phylogenetic tree shown in Fig. <xref rid="Fig1" ref-type="fig">1</xref>. All branches received maximum support, except for that between <italic>A. niger</italic> strains NRRL2 and ATCC 1015 (73%; Fig. <xref rid="Fig1" ref-type="fig">1b</xref>).</p></sec><sec id="Sec47"><title>Identification of clusters of orthologous genes</title><p>Clusters of orthologous genes were identified using OrthMCL with an inflation value of 1.5 [<xref ref-type="bibr" rid="CR276">276</xref>]. All other parameters, e.g., BLAST search, were used in the default settings.</p></sec></sec><sec id="Sec48"><title>Identification/annotation of specific gene sets</title><sec id="Sec49"><title>Genes involved in asexual and sexual reproduction</title><p>The annotation pipeline of putative genes involved in asexual and sexual sporulation involved a two-step procedure of identification and annotation. Genes previously identified from <italic>A. nidulans</italic> were used as references (Additional files <xref rid="MOESM2" ref-type="media">2</xref> and <xref rid="MOESM5" ref-type="media">5</xref>). The identification step of asexual genes was performed by searching the reference protein sequences against Aspergillus overall protein sequences with phmmer of HMMER 3.0 (<ext-link ext-link-type="uri" xlink:href="http://hmmer.org/">http://hmmer.org/</ext-link>). Hits that passed MSV, Bias, Vit, and Fwd filters (see HMMER User’s Guide, <ext-link ext-link-type="uri" xlink:href="http://eddylab.org/">http://eddylab.org/</ext-link>) were then subject to annotation involving BlastP comparisons against the database of non-redundant protein sequences [<xref ref-type="bibr" rid="CR277">277</xref>] (Additional file <xref rid="MOESM2" ref-type="media">2</xref>). The identification of sexual genes was performed by searching protein databases available at the JGI (<ext-link ext-link-type="uri" xlink:href="http://genome.jgi.doe.gov/">http://genome.jgi.doe.gov/</ext-link>) or AspGD (<ext-link ext-link-type="uri" xlink:href="http://www.aspergillusgenome.org/">http://www.aspergillusgenome.org/</ext-link>) websites by BLASTP interrogation. Hits that had a minimum E value of 1e<sup>–70</sup> were considered significant except for analysis of the relatively short PpgA protein where less stringent criteria were applied (Additional file <xref rid="MOESM5" ref-type="media">5</xref>). Synteny analysis (SYBIL) was then performed using the Jaccard Orthologous cluster option at AspGD or synteny option at the JGI website. Based on high levels of similarity and/or a large functional homogeneity of the hits, predicted proteins were annotated as corresponding functional proteins.</p></sec><sec id="Sec50"><title>Genes involved in organic acid production</title><p>For determination of isoenzymes in production of organic acids, a list of known and predicted isoenzymes from <italic>A. niger</italic> CBS 513.88 was used as the seeding set. Using a BLAST-comparison, all genes above a cutoff value of 80% identity and 80% coverage were recorded as isoenzymes for the individual species.</p></sec><sec id="Sec51"><title>Prediction and synteny analysis of aspergilli SM clusters</title><p>Protein and genomic sequences of aspergilli were downloaded from AspGD (<ext-link ext-link-type="uri" xlink:href="http://www.aspgd.org/">http://www.aspgd.org/</ext-link>). Detection of PKS, NRPS, and DMATs and further prediction of respective SM gene clusters were made with SMIPS and CASSIS tools, correspondingly (<ext-link ext-link-type="uri" xlink:href="https://sbi.hki-jena.de/cassis/">https://sbi.hki-jena.de/cassis/</ext-link>) Synteny analysis was performed with the help of an <italic>Aspergillus</italic> 21-way comparative database asp2_v9 powered by Sybil. Conservation of clusters was calculated as the percentage of genes in the query cluster conserved in the syntenic counterpart. Confirmation of the identity of different secondary metabolites from the aspergili were checked by ultra high performance liquid chromatography–diode array detection–high resolution mass spectrometric detection (UHPLC-DAD-HRMS) [<xref ref-type="bibr" rid="CR278">278</xref>].</p></sec><sec id="Sec52"><title>Analysis of CYP proteins</title><p>Evolutionary analyses were conducted in MEGA5 [<xref ref-type="bibr" rid="CR279">279</xref>]. The analysis involved 19 amino acid sequences. If protein size is marked by a star, the sequence was manually curated or sequences are incomplete. Following MUSCLE alignment, the evolutionary history was inferred by using the maximum likelihood method based on the JTT matrix-based model [<xref ref-type="bibr" rid="CR280">280</xref>]. There was a total of 496 (CYP51F1) or 510 (CYP53) positions in the final dataset. The tree is drawn to scale, with branch lengths measured in the number of substitutions per site. All positions containing gaps and missing data were eliminated. Additional copies of CYP51F2 and CYP51F4 are excluded from the tree.</p></sec><sec id="Sec53"><title>Aspergillus sugar transportome</title><p>The assignment of a protein to the “Sugar and other transporters” PFAM family PF00083 is based on its level of similarity to a Hidden Markov Model (HMM). The HMM for PF00083 is derived from a seed alignment of 33 proteins chosen to be the core representatives of that family [<xref ref-type="bibr" rid="CR281">281</xref>, <xref ref-type="bibr" rid="CR282">282</xref>]. The latter includes proteins for which either transport of a specific sugar or related substrate has been experimentally demonstrated, or there is very strong indirect evidence that such a transport function exists, e.g. genetic evidence. Despite their considerable diversity in primary structure, PF00083 members exhibit a common topology of 12 membrane-spanning domains (TMSs) divided into two groups of six. Transmembrane (TM) domain predictions were obtained for all the PF00083-annotated proteins studied using TMHMM v2 [<xref ref-type="bibr" rid="CR283">283</xref>]. While the majority of protein sequences exhibited 2 × 6 TM topology, we manually reannotated some <italic>loci</italic> to yield greater consensus with the 12 TM topology and a very small number were excluded from further analysis due to the detection of fewer than three TM domains. The resulting collection of amino acid sequences was aligned by MUSCLE and a neighbor-joining (NJ) tree was generated using MEGA6 software [<xref ref-type="bibr" rid="CR284">284</xref>]. Cluster analysis was also performed using the orthology detection tool “Proteinortho”) [<xref ref-type="bibr" rid="CR285">285</xref>] and the results obtained found to be concordant with the identifications made in the NJ tree.</p></sec><sec id="Sec54"><title>Amino acid and urea transporters</title><p>The high-affinity methionine transporter of <italic>S. cerevisiae</italic> (MUP1) was used to identify several close homologs in all <italic>Aspergillus</italic> species. The methionine transporters of <italic>S. cerevisiae</italic> belong to the L-type amino acid transporter family (LAT; TCDB 2.A.3.8) [<xref ref-type="bibr" rid="CR140">140</xref>] and exhibit low similarity to YATs [<xref ref-type="bibr" rid="CR286">286</xref>]. <italic>A. nidulans</italic> UreA [[<xref ref-type="bibr" rid="CR183">183</xref>, <xref ref-type="bibr" rid="CR184">184</xref>] was used to search the fungal genomes analyzed in this study for the presence of urea-like transporters (Table <xref rid="Tab5" ref-type="table">5</xref>).</p><p>The <italic>S. cerevisiae</italic> proteins Tat1, Tat2, Tat3, Gap1, Hip1, Gnp, Agp1, Agp2, Agp3, Bap2, Bap3, Sam3, Mmp1, Lyp1, Alp1, Can1, Dip5, Put4, and Ssy1 obtained from the <italic>Saccharomyces</italic> Genome Database [<xref ref-type="bibr" rid="CR287">287</xref>] were used as in silico probes for BlastP and in several cases, TBlastN searches in the available <italic>Aspergillus</italic> genomes at either the AspGD [<xref ref-type="bibr" rid="CR14">14</xref>] or the JGI [<xref ref-type="bibr" rid="CR15">15</xref>] databases. In addition, the homologues obtained for <italic>A. nidulans</italic> were used as in silico probes in a second BlastP search round. We have also identified a number of pseudo genes, either because their coding sequence contains frameshift and/or early chain termination mutations (ANID_4604, ANID_8556, ANID_8659, AFL2G_12189, AO090103000195, AO090005000021, AFL2G_06574, AO090026000738). In three other paralogues (ANID_5024, Aspbr1_139443, and Aspwe1_115075), the coding sequences lack a significant part of a functional YAT transporter [<xref ref-type="bibr" rid="CR288">288</xref>]. These could be also considered pseudo genes or may have been recruited to a different function. Interestingly, no transcripts at all are detected (Jbrowse, [<xref ref-type="bibr" rid="CR14">14</xref>]) for ANID_5024 and the adjacent gene (ANID_5023) in complete medium, while the genes on either side are transcribed under these conditions.</p><p>Alignment was done with MAFFT, Auto mode, Blosum62. Curation was carried out with BMGE. The tree shown was obtained using Blosum30 as a similarity matrix, but a topologically identical tree was obtained using the more stringent Blosum62 similarity matrix default setting. The maximum likelihood rooted tree was obtained with PhyML. The final tree with collapsed branches was drawn with FigTree.</p></sec><sec id="Sec55"><title>Nucleobase transporters</title><p>The alignment of these putative transporters was performed using MAFFT [<xref ref-type="bibr" rid="CR289">289</xref>]; curation was with BMGE [<xref ref-type="bibr" rid="CR290">290</xref>] with a Blosum30 substitution matrix. Phylogeny was performed with PhyML [<xref ref-type="bibr" rid="CR291">291</xref>] and re-drawing of the tree with FigTree [<xref ref-type="bibr" rid="CR292">292</xref>].</p></sec><sec id="Sec56"><title>Identification of protein class members involved in signal transduction</title><p>We employed a domain-based approach for the identification of proteins for each class, i.e. G-proteins, GPCRs, kinases, and phosphatases, following the general approach described by Perez-Rodriguez et al. [<xref ref-type="bibr" rid="CR293">293</xref>] and using the pipeline available at [<xref ref-type="bibr" rid="CR294">294</xref>]. The most important step is the identification of a protein domain or block that is characteristic of the protein class/family of interest and that is represented as a HMM, either available in the public database PFAM or created in house. Then specific rules are built accounting for the domain architecture of the different families/classes, in an exclusive way, i.e. a protein can belong to one and only one family/class, which requires the introduction of forbidden domains to resolve ties (Additional file <xref rid="MOESM36" ref-type="media">36</xref>). The HMMs used for the identification of protein classes of interest are available as (Additional file <xref rid="MOESM37" ref-type="media">37</xref>). Classification results are available in Additional file <xref rid="MOESM31" ref-type="media">31</xref>.</p><sec id="FPar3"><title>G-proteins</title><p>We studied the three sub-units of G-protein complexes: alpha, beta, and gamma. G-alpha and G-gamma had already well-described, characteristic, and specific domains in the PFAM database [<xref ref-type="bibr" rid="CR282">282</xref>] with accession numbers PF00503 and PF00631, respectively. The G-beta subunit has several copies of the WD40 repeat (PF00400); however, this domain is not specific for G-beta proteins. We assesed the accuracy of our classification comparing our results against those presented in Li et al. [<xref ref-type="bibr" rid="CR227">227</xref>]. The G-gamma famly is always found as a single member in each species. However, following our domain-based apporach we could not find the corresponding protein in <italic>A. niger</italic> CBS 513.88, <italic>A. oryzae</italic>, and <italic>S. pombe</italic>. Further inspection revealed that the protein is not annotated in the <italic>Aspergillus</italic> genomes, but we found a genomic region with the information for this gene, using the <italic>A. nidulans</italic> protein sequence as bait in a BLAST search (Additional file <xref rid="MOESM37" ref-type="media">37</xref>). In the case of <italic>S. pombe</italic>, the G-gamma subunit appears to be missing from the current version of the genome sequence.</p></sec><sec id="FPar4"><title>GPCRs</title><p>For the identification of GPCRs, we took as gold standard the list provided by Li et al. [<xref ref-type="bibr" rid="CR227">227</xref>] for <italic>A. nidulans</italic>. For some of the families (Stm1-related, GprK-like, PTH11, MG00532-like, material available under request) we built specific HMMs able to retrieve all of the known members of the respective family in <italic>A. nidulans</italic> and then applied them to the other species. Only in the case of PTH11 did we identify more members than the ones listed in the gold standard.</p></sec><sec id="FPar5"><title>Kinases</title><p>We used as gold standard the identification and classification of kinases in <italic>A. nidulans</italic> from de Souza et al. [<xref ref-type="bibr" rid="CR233">233</xref>]. All kinase classes have characteristic and specific domains available in PFAM, except the TOR kinases. We built an HMM specific for TOR kinases as described in Additional files <xref rid="MOESM37" ref-type="media">37</xref> and <xref rid="MOESM38" ref-type="media">38</xref>.</p></sec><sec id="FPar6"><title>Classical Ser/Thr phosphatases (PPP and PTP)</title><p>All PPPs in <italic>A. nidulans</italic> have the PFAM domain Metallophos (PF00149), but this domain also appears in other proteins. We retrieved all <italic>A. nidulans</italic> proteins that had a hit to the Metallophos domain and inferred the phylogeny, reveling that PPPs form a distinct clade in this evolutionary tree (Additional file <xref rid="MOESM39" ref-type="media">39</xref>), thus allowing us to build a PPP-specific HMM, named PP2Ac. In the case of the PPM family there were already specific PFAM domains that could be used to develop classification rules (Additional file <xref rid="MOESM36" ref-type="media">36</xref>).</p></sec><sec id="FPar7"><title>PTPs</title><p>For most PTP superfamily members in [<xref ref-type="bibr" rid="CR236">236</xref>] there were already specific domains in PFAM, i.e. Y_phosphatase, Y_phosphatase2, Y_phosphatase3, DSPc, and LMWPc. AN3941, belonging to the CDC25 subclass, was the unique PTP with no specific Pfam domain. Thus, we built a specific HMM (CTBECDC25) for this protein phosphatase. Although SSU72 proteins share sequence similarity with the PTP superfamily, they are classified as a distinct type of protein phosphatases. In that case, we used this PFAM domain Ssu72 Pfam for their identification.</p></sec><sec id="FPar8"><title>Asp-based protein phosphatases</title><p>Aspartate-based catalysis phosphatases, which share the DXDXT/V catalytic signature (CPDs), had a specific domain found in the PFAM database, i.e. NIF (PF03031).</p></sec></sec><sec id="Sec57"><title>Histones of the aspergilli</title><p>Initial searches for histone H1 by BlastP failed to locate matches in some <italic>Aspergillus</italic> databases, while in other species the gene model was incorrect. Therefore, manual curation was required to establish its presence in <italic>A. oryzae</italic> and correction of the amino acid sequences was required for <italic>A. brasiliensis</italic>, <italic>A. kawachii</italic>, <italic>A. sydowii</italic>, <italic>A. terreus</italic>, <italic>A. versicolor</italic>, and <italic>A. niger</italic> CBS513.88. The NCBI database for <italic>Aspergillus sojae</italic> was interrogated to search for histone proteins in this species. Manual corrections of the H3 histone gene models were required for <italic>A. niger</italic> CBS 513.88, <italic>A. wentii</italic>, and <italic>A. aculeatus</italic>.</p></sec></sec><sec id="Sec58"><title>Data access</title><p>Genome assembly and annotations are available at at the JGI fungal genome portal MycoCosm [<xref ref-type="bibr" rid="CR15">15</xref>] and have been deposited at DDBJ/EMBL/GenBank under the following accessions: <italic>A. aculeatus</italic> ATCC16872 - MRCK00000000, <italic>A. brasiliensis</italic> CBS101740 - LJXV00000000, <italic>A. carbonarius</italic> ITEM5010 - AHIG00000000, <italic>A. foetidus</italic> CBS106.47 - MRBP00000000, <italic>A. glaucus</italic> CBS516.65 - LSTL00000000, <italic>A. sydowii</italic> CBS593.65 - MRCH00000000, <italic>A. tubingensis</italic> CBS134.48 - LJXU00000000, <italic>A. versicolor</italic> CBS583.65 - MRBN00000000, <italic>A. wentii</italic> CBS141173 (DTO134E9) - LJSE00000000, and <italic>A. zonatus</italic> CBS506.65 - MRBM00000000. Links to the raw genome and transcriptome data of these species are available in Additional file <xref rid="MOESM1" ref-type="media">1</xref>D. This also lists the genbank (if available) and JGI accession numbers of the genomes used for comparison as well as the papers in which they have been published.</p><p>Proteomics data of the wheat bran and sugar beet cultures are available via ProteomeXchange with identifier PXD005563. Proteomics data for the stress experiments are available at <ext-link ext-link-type="uri" xlink:href="http://wwwuser.gwdg.de/~hkusch/GBIO_DeVries/">http://wwwuser.gwdg.de/~hkusch/GBIO_DeVries/</ext-link>.</p></sec><sec id="Sec59"><title>Expression of mating-type and pheromone-signaling pathway genes</title><p>Representative asexual species (<italic>A. luchuensis</italic> (<italic>A. acidus</italic>, <italic>A. foetidus</italic>), <italic>A. aculeatus</italic>, <italic>A. brasilliensis</italic>, <italic>A. carbonarius</italic>, <italic>A. clavatus</italic>, <italic>A. niger</italic>, <italic>A. sydowii</italic>, <italic>A. versicolor</italic>, <italic>A. wentii</italic>, <italic>A. zonatus</italic>), together with some control sexual species (<italic>A. flavus</italic>, <italic>A. fumigatus</italic>, <italic>A. tubingensis</italic>), were selected for experimental work to assess possible expression of mating-type (<italic>MAT</italic>) and pheromone-signaling pathway (<italic>ppgA</italic>, <italic>preA</italic>, and <italic>preB</italic>) genes. Identified <italic>MAT1-1</italic>, <italic>MAT1-2</italic>, <italic>ppgA</italic>, <italic>preA</italic>, and <italic>preB</italic> sequences were used to design primers for (RT)-PCR investigations (primer sequences available on request). Primers were designed ideally either side of an intron to allow differentiation of genomic or cDNA products by resulting product sizes. Genomic DNA was extracted from all species using a Nucleospin® Plant II kit (Macherey-Nagel). Cultures were grown in <italic>Aspergillus</italic> complete media (ACM) broth [<xref ref-type="bibr" rid="CR46">46</xref>] at 28 °C with shaking for two days. Cultures were harvested by filtration through a sterile miracloth filter (Millipore) and washed with a pH 7.5 phosphate buffer solution, then freeze-dried and ground under liquid nitrogen into powder by motor and pestle. After quantification, 50 ng was used as a DNA template for subsequent PCR. To evaluate possible transcription of genes, RNA was extracted from cultures of all test species grown on solid media under conditions known to be favourable for sex in the aspergilli. Nylon filter membranes (pore size 0.2 μm) were placed over the surface of 5 cm Petri dishes containing 10 mL of oat meal agar (N.B. This media was used for all species except for <italic>A. versicolor</italic>, which did not grow well on this substrate. ACM agar was instead used for <italic>A. versicolor</italic>). A total of 50 μL of a spore suspension (containing 1 × 10<sup>5</sup> conidia) was spread over the surface and cultures incubated in the dark at 32 °C. Plates were then sealed with two layer of Parafilm after 15–18 h of incubation [<xref ref-type="bibr" rid="CR46">46</xref>]. Mycelia were then scraped off the surface of the filters after either four or eight days, dried using sterile paper tissue, and then flash frozen under liquid nitrogen. For most species, RNA extracted was then extracted using a TRizol method according to manufacturer’s instructions (Thermo Fisher). However, a CTAB method (Heather Darbyshir pers comm) was used for RNA extraction from members of the black aspergilli taxonomic grouping. For both methods, a Nucleospin® RNA extraction kit (Macherey-Nagel) was used for clean-up of the extracted RNA. After quantification, the extracted RNA was checked on agarose gel for purity and integrity of RNA. CDNA synthesis from all extracted RNA for all of species was achieved using Superscript<sup>TM</sup> III; 500 ng of total RNA was used for cDNA synthesis, and then 1 μL of cDNA was used for subsequent amplifications. Final PCR was performed using a Phusion High Fidelity PCR kit according to manufacturer’s instructions (New England Biolabs). One microliter of each genomic DNA and cDNA from four-day-old and eight-day-old cultures were used as a template for amplification of <italic>MAT1-1</italic>, <italic>MAT1-2</italic>, <italic>ppgA</italic>, <italic>preA</italic>, and <italic>preB</italic> genes. In addition, expression of the <italic>actA</italic> (actin) gene was monitored as a control “housekeeping” gene. PCR products were resolved on 2.0–2.5% agarose gels. Successful amplification of all mating-type and pheromone-signaling pathway genes was achieved for for all species except for the <italic>MAT1-2</italic> gene of <italic>A. versicolor</italic>, which could not be amplified despite use of multiple primer sets and this gene was therefore excluded from the analysis.</p></sec><sec id="Sec60"><title>Growth profiling on different nutrient sources</title><p>For growth profiling, all strains were grown on MM [<xref ref-type="bibr" rid="CR295">295</xref>] containing monosaccharides/oligosaccharides, polysaccharides, and crude substrates at 25 mM, 1%, and 3% final concentration, respectively. Cultures for proteomics were performed in MM with 1% wheat bran or 1% sugar beet pulp, as previously described [<xref ref-type="bibr" rid="CR57">57</xref>], and proteomics was performed as described in that paper. For laccase and cellobiose dehydrogenase activity, the 20 aspergilli were grown in duplicate in liquid shaken cultures at 30 °C, 120 rpm. A total of 250 mL baffled erlenmeyers filled with 50 mL of MM [<xref ref-type="bibr" rid="CR295">295</xref>] and supplemented with 10 g of cotton seed hulls were inoculated with 2 × 10<sup>6</sup> spores/mL final concentration.</p></sec><sec id="Sec61"><title>Stress tolerance studies</title><p>In the stress tolerance studies, 18 <italic>Aspergillus</italic> strains with fully sequenced fungal genomes representing 17 species were included (Additional files <xref rid="MOESM3" ref-type="media">3</xref> and <xref rid="MOESM4" ref-type="media">4</xref>). For the production of conidia, normally the malt extract—mycological pepton sporulation agar medium (1.5% agar)—recommended by CBS-KNAW (<ext-link ext-link-type="uri" xlink:href="http://www.fung-stress.org/">http://www.fung-stress.org/</ext-link>) was used. The sporulation medium for <italic>A. glaucus</italic> was also supplemented with 1.0 M NaCl. Unless otherwise indicated, asexual sporulation was carried out at 25 °C in the dark for six days. <italic>A. fumigatus</italic> and <italic>A. nidulans</italic> were also sporulated on the CBS-KNAW medium at 37 °C and on nitrate minimal medium agar plates (NMM, solidified with 1.8% agar) [<xref ref-type="bibr" rid="CR296">296</xref>] at 37 °C. Microbial growth and stress sensitivity assays were performed on NMM agar plates (1.8% VWR International Agar powder for bacteriology, ID number 20 767.298), which were incubated at 25 (5 or 10 d) or 37 °C (5 d) in the dark and were supplemented with the stress-initiating agents H<sub>2</sub>O<sub>2</sub> (oxidative stress), menadione sodium bisulfite (MSB, oxidative stress), NaCl (ionic osmotic stress), sorbitol (non-ionic osmotic stress), Congo Red (cell wall integrity stress), or CdCl<sub>2</sub> (heavy metal stress) as required (Additional files <xref rid="MOESM3" ref-type="media">3</xref> and <xref rid="MOESM4" ref-type="media">4</xref>; [<xref ref-type="bibr" rid="CR133">133</xref>]). We typically performed two to three sets of experiments (often more) with spores harvested from independent sporulations for each stress condition. Each set contained 4-4 replicates. We took photos of the most representative colonies.</p><p>Stress agar plates were inoculated and, after completing the physiological experiments, the fungal colonies were photographed as described before [<xref ref-type="bibr" rid="CR297">297</xref>]. Fungal growth was characterized either by colony diameters or by scoring them by eye on a 0–10 scale (Additional files <xref rid="MOESM3" ref-type="media">3</xref> and <xref rid="MOESM4" ref-type="media">4</xref>). Stress sensitivities were quantified by percentage decreases in the colony diameters in comparison to controls or by decreases in the growth scores. Based on the growth inhibition values, all species tested were ranked according to their stress tolerances (Additional file <xref rid="MOESM4" ref-type="media">4</xref>). Physiological data have been stored in the Fungal Stress Database (FSD; <ext-link ext-link-type="uri" xlink:href="http://www.fung-stress.org/">http://www.fung-stress.org/</ext-link>) at CBS-KNAW. Stress response proteins were identified and annotated in the newly sequenced <italic>Aspergillus</italic> genomes following the procedure described previously [<xref ref-type="bibr" rid="CR298">298</xref>] and newly identified orthologs were inserted into the Fungal Stress Response Database (FSRD) - version 2 [<xref ref-type="bibr" rid="CR298">298</xref>] (FSRDv_2; <ext-link ext-link-type="uri" xlink:href="http://internal.med.unideb.hu/fsrd2/?p=consortium">http://internal.med.unideb.hu/fsrd2/?p=consortium</ext-link>). The phylogeny of selected well-characterized stress response proteins and their orthologs was studied following the procedure described in Additional file <xref rid="MOESM3" ref-type="media">3</xref>.</p></sec><sec id="Sec62"><title>Enzyme assays</title><p>For analysis of oxidative enzymes, the 20 aspergilli were grown in duplicate in liquid shaken cultures at 30 °C, 120 rpm. A total of 250 mL baffled erlenmeyers filled with 50 mL of medium were inoculated with to a final concentration of 2 × 10<sup>6</sup> spores/mL. MM (for 1000 L: 6 g NaNO<sub>3</sub>, 1.5 g KH<sub>2</sub>PO<sub>4</sub>, 0.5 g KCl, 0.5 g MgSO<sub>4</sub>.7H2O, trace elements, CuSO<sub>4</sub> 0.02 g, pH 6.0) was supplemented with 10 g of cotton seed hulls as the carbon source. Laccase activity in the culture supernatant was assayed by monitoring the oxidation of 500 μM ABTS at 420 nm to the respective radical (ε420 = 36 mM-1 cm-1) [<xref ref-type="bibr" rid="CR299">299</xref>], in the presence of 50 mM sodium tartrate pH 4.0 at 30 °C.</p><p>The CDH activity was determined at 30 °C, using 0.2 mM 2,6-dichlorophenol indophenol (DCPIP) in 50 mM sodium acetate buffer, pH 5, in the presence of cellobiose 10 mM as the substrate [<xref ref-type="bibr" rid="CR300">300</xref>]. The decrease in absorption of DCPIP (ε = 68,000 M-1 cm-1) was monitored at 520 nm for 30 s.</p></sec><sec id="Sec63"><title>Functionality of P450 proteins and NO sensitivity</title><p>Functionality of P450 proteins was tested by growing mycelia of aspergilli on MBFA agar supplemented with 0.02 mM ketoconazole or 2 mM benzoic acid. Inhibition of growth (Inhib.) as a percentage of the control without supplementation (Contr.) was determined. For nitric oxide sensitivity, all 19 species were cultivated in liquid MM containing 1% glucose and 10 mM ammonium tartrate in microtiter plates. Only medium used for <italic>A. niger</italic> CBS 513.88 was supplemented with a vitamin solution (80 mg/L <italic>p</italic>-aminobenzoic acid, 50 mg/L thiamin HCl, 1 mg/L biotin, 400 mg/L inositol, 100 mg/L nicotinic acid, 200 mg/L calcium pantothenate, 100 mg/L riboflavin, 50 mg/L pyridoxine). The liquid medium was supplemented with different concentrations of sodium nitroprusside (SNP): 0 (control samples), 16, 64, or 128 mM. A total of 1 × 10<sup>4</sup> spores of each organism in a final volume of 150 μL per well was used as a replicate. Four replicates were done per organism per treatment. All fungi were incubated at 30 °C except for <italic>A. glaucus</italic>, which was grown at 22 °C. Absorbance was recorded at 492 nm every 24 h in an Axis expert plus plate reader. Percentage of growth inhibition was calculated comparing absorbance values at 0 versus 128 mM SNP. Growing time for calculations was in the range of 48–96 h depending on each organism (see Fig. <xref rid="Fig11" ref-type="fig">11</xref> legend). Final values shown are the average of two independent experiments with four replicates per experiment.</p></sec><sec id="Sec64"><title>Functional analysis of sugar transporters</title><p>cDNA clones of the transporter genes were amplified by PCR and cloned into pYEX-BX using DNA ligase according to the manufacturer’s instructions. Sequence analysis was used to verify the correct clones. <italic>S. cerevisiae</italic> tester strains used were: KY73 [<xref ref-type="bibr" rid="CR301">301</xref>], EB.VW4000 [<xref ref-type="bibr" rid="CR302">302</xref>], MaDH4 [<xref ref-type="bibr" rid="CR303">303</xref>], SEY6210 [<xref ref-type="bibr" rid="CR304">304</xref>], CMY1050 [<xref ref-type="bibr" rid="CR305">305</xref>]. Plasmids were derived from pYEX-BX (Clontech) [<xref ref-type="bibr" rid="CR306">306</xref>]. Plasmid transformations of yeast cells were carried out according to the quick and easy TRAFO protocol [<xref ref-type="bibr" rid="CR307">307</xref>]. Ten milliliters of YNB + 2% maltose supplemented as described above, was inoculated with a single yeast colony and grown overnight (16 h) at 30 °C and 250 rpm in an orbital shaker. OD<sub>500</sub> measurements were taken for all cultures. The cells were centrifuged at 10,000 rpm for 10 s and, after the supernatant was removed, resuspended in MilliQ water. Cells were washed twice in this manner. A final centrifugation step (10,000 rpm for 10 s) was followed by resuspension in sufficient MilliQ water to result in a cell suspension with an OD of 0.1 (approx. 10<sup>4</sup> cells/mL). NUNC 96-well optical bottom plates polymer base microtitre plates, containing media as described above, were inoculated with approximately 10<sup>2</sup> cells to a final volume of 100 uL in a sterile manner. Plates were sealed using breathable seals and incubated at 28 °C. Growth was monitored by OD<sub>590</sub> measurements taken at 0, 24, 48, 72, 96, and 120 h time points.</p></sec></sec></body><back><app-group><app id="App1"><sec id="Sec65"><title>Additional files</title><p><media position="anchor" xlink:href="13059_2017_1151_MOESM1_ESM.xlsx" id="MOESM1"><label>Additional file 1:</label><caption><p>Genome statistics and information. (XLSX 97 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM2_ESM.xlsx" id="MOESM2"><label>Additional file 2:</label><caption><p>Summary of putative genes related to asexual sporulation in tested strains. (XLSX 20 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM3_ESM.xls" id="MOESM3"><label>Additional file 3:</label><caption><p>Stress response in Aspergilli. (XLS 619 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM4_ESM.xlsx" id="MOESM4"><label>Additional file 4:</label><caption><p>Summary of putative genes related to mating and pheromone signalling in tested strains. (XLSX 12 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM5_ESM.pdf" id="MOESM5"><label>Additional file 5:</label><caption><p>Expression of mating and pheromone-signalling pathway genes in representative asexual aspergilli. (PDF 488 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM6_ESM.pdf" id="MOESM6"><label>Additional file 6:</label><caption><p>Overview of number of putative orthologs/paralogs in the compared fungal species related to primary carbon metabolism. (PDF 237 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM7_ESM.pdf" id="MOESM7"><label>Additional file 7:</label><caption><p>Comparative growth profiling of the aspergilli and selected other fungi. (PDF 8.65 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM8_ESM.pdf" id="MOESM8"><label>Additional file 8:</label><caption><p>Effect of SHAM and KCN on fungal growth and sporulation. (PDF 252 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM9_ESM.xlsx" id="MOESM9"><label>Additional file 9:</label><caption><p>Organic acid production. (XLSX 40 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM10_ESM.xlsx" id="MOESM10"><label>Additional file 10:</label><caption><p>CAZy comparison of the species. (XLSX 30 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM11_ESM.xlsx" id="MOESM11"><label>Additional file 11:</label><caption><p>Orthology analysis of CAZy genes related to plant biomass degradation. (XLSX 148 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM12_ESM.xlsx" id="MOESM12"><label>Additional file 12:</label><caption><p>Laccase and cellobiose dehydrogenase (CDH) activities of the selected aspergilli. (XLSX 11 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM13_ESM.pdf" id="MOESM13"><label>Additional file 13:</label><caption><p>Molecular phylogenetic tree of CYP56 family (A), and CPR2 and CYP630 family (B). (PDF 402 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM14_ESM.pdf" id="MOESM14"><label>Additional file 14:</label><caption><p>Molecular phylogenetic tree of CYP6001 - CYP6003 families (PpoA - PpoD) and colinearity of the genetic surroundings. (PDF 279 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM15_ESM.pdf" id="MOESM15"><label>Additional file 15:</label><caption><p>Extended analysis of stress tolerance of the aspergilli. (PDF 706 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM16_ESM.xls" id="MOESM16"><label>Additional file 16:</label><caption><p>Orthologs of selected stress response proteins. (XLS 76 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM17_ESM.pdf" id="MOESM17"><label>Additional file 17:</label><caption><p>Extended analysis of stress tolerance of the aspergilli (2). (PDF 1842 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM18_ESM.xlsx" id="MOESM18"><label>Additional file 18:</label><caption><p>Identified secreted proteins (<italic>A. sydowii</italic>, <italic>A. tubingensis</italic>, <italic>A. wentii</italic>, <italic>A. zonatus</italic>). (XLSX 34 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM19_ESM.xlsx" id="MOESM19"><label>Additional file 19:</label><caption><p>Strain specific PFAM domains predicted for identified secreted proteins (<italic>A. sydowii</italic>, <italic>A. tubingensis</italic>, <italic>A. wentii</italic>, <italic>A. zonatus</italic>). (XLSX 12 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM20_ESM.xlsx" id="MOESM20"><label>Additional file 20:</label><caption><p>Distribution of putative sugar transporters. (XLSX 17 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM21_ESM.xlsx" id="MOESM21"><label>Additional file 21:</label><caption><p>Detailed overview of putative sugar transporters in the aspergilli. (XLSX 10790 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM22_ESM.xlsx" id="MOESM22"><label>Additional file 22:</label><caption><p>Functional analysis of <italic>A. niger</italic> sugar transporters by complementation of <italic>S. cerevisiae</italic> transport mutant strains. (XLSX 12 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM23_ESM.pdf" id="MOESM23"><label>Additional file 23:</label><caption><p>Maximum likelihood tree of YAT transporters in the aspergilli. (PDF 89 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM24_ESM.pdf" id="MOESM24"><label>Additional file 24:</label><caption><p>Phylogenetic relationships of UreA homologs. (PDF 108 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM25_ESM.pdf" id="MOESM25"><label>Additional file 25:</label><caption><p>CLUSTAL O(1.2.3) multiple sequence alignment of NNP nitrate transporters. (PDF 149 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM26_ESM.pdf" id="MOESM26"><label>Additional file 26:</label><caption><p>Maximum likelihood rooted tree of Fur-like transporters of the aspergilli and some other members of the Eurotiales (<italic>Penicillium</italic>, <italic>Talaromyces</italic>). (PDF 537 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM27_ESM.pdf" id="MOESM27"><label>Additional file 27:</label><caption><p>Maximum likelihood rooted phylogeny of the FCY-like transporters of the aspergilli and some penicillia. (PDF 324 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM28_ESM.pdf" id="MOESM28"><label>Additional file 28:</label><caption><p>Number of flavohemoglobins and protein IDs found in the genome sequences of the <italic>Aspergillus</italic> species. (PDF 79 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM29_ESM.xlsx" id="MOESM29"><label>Additional file 29:</label><caption><p>Species-specific signal transduction pathway genes in Eurotiomycetes. (XLSX 14 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM30_ESM.xlsx" id="MOESM30"><label>Additional file 30:</label><caption><p>Predicted G-proteins and GPCRs proteins in the Eurotiomycetes. (XLSX 16 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM31_ESM.xlsx" id="MOESM31"><label>Additional file 31:</label><caption><p>Classification and Clusters of signal transduction related genes. (XLSX 1577 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM32_ESM.xlsx" id="MOESM32"><label>Additional file 32:</label><caption><p>Distribution of SRPKs in Eurotiomycetes. (XLSX 11 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM33_ESM.pdf" id="MOESM33"><label>Additional file 33:</label><caption><p>Kinases presented in at least one yeast species and with no orthologous genes in other eurotiomycetes. (PDF 117 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM34_ESM.pdf" id="MOESM34"><label>Additional file 34:</label><caption><p>Histones of the Aspergilli. (PDF 526 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM35_ESM.pdf" id="MOESM35"><label>Additional file 35:</label><caption><p>Maximal likelihood phylogeny of MASC1/RID1 orthologs. (PDF 115 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM36_ESM.txt" id="MOESM36"><label>Additional file 36:</label><caption><p>Introduction of forbidden domains for the HMM analysis of signal transduction genes. (TXT 806 bytes)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM37_ESM.hmms" id="MOESM37"><label>Additional file 37:</label><caption><p>HMM file used for the identification of protein classes of interest related to signal transduction. (HMMS 4334 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM38_ESM.xlsx" id="MOESM38"><label>Additional file 38:</label><caption><p>Unannotated genes related to signal transduction. (XLSX 8 kb)</p></caption></media><media position="anchor" xlink:href="13059_2017_1151_MOESM39_ESM.pdf" id="MOESM39"><label>Additional file 39:</label><caption><p>Phylogeny of the Methallophos domain in <italic>A. nidulans</italic>. (PDF 96 kb)</p></caption></media></p></sec></app></app-group><glossary><title>Abbreviations</title><def-list><def-item><term>AA</term><def><p>Auxiliary activity</p></def></def-item><def-item><term>AAAP</term><def><p>Amino acid/auxid permease</p></def></def-item><def-item><term>AspGD</term><def><p>Aspergillus Genome Database</p></def></def-item><def-item><term>CAZy</term><def><p>Carbohydrate Active enzyme database</p></def></def-item><def-item><term>CE</term><def><p>Carbohydrate esterase</p></def></def-item><def-item><term>CYP</term><def><p>Cytochrome P450</p></def></def-item><def-item><term>GH</term><def><p>Glycoside hydrolase</p></def></def-item><def-item><term>GPCR</term><def><p>G-protein-coupled receptor</p></def></def-item><def-item><term>H1</term><def><p>Histone 1</p></def></def-item><def-item><term>H2</term><def><p>Histone 2</p></def></def-item><def-item><term>H3</term><def><p>Histone 3</p></def></def-item><def-item><term>H4</term><def><p>Histone 4</p></def></def-item><def-item><term>JGI</term><def><p>Joint Genome Institute</p></def></def-item><def-item><term>MFS</term><def><p>Major Facilitator Superfamily</p></def></def-item><def-item><term>NO</term><def><p>Nitric oxide</p></def></def-item><def-item><term>PL</term><def><p>Polysaccharide lyase</p></def></def-item><def-item><term>SM</term><def><p>Secondary metabolite</p></def></def-item><def-item><term>SSS</term><def><p>Solute symporter family</p></def></def-item><def-item><term>TMD</term><def><p>Transmembrane domain</p></def></def-item></def-list></glossary><ack><title>Acknowledgements</title><p>Members of the University of Debrecen were supported financially by the Hungarian Scientific Research Fund (grant K100464 to IP) as well as by the TÁMOP 4.2.1./B-09/1/KONV-2010-0007 and SROP-4.2.2.B-15/1/KONV-2015-0001 projects, which were supported by the European Union, co-financed by the European Social Fund. EO was a recipient of a Campus Hungary Programme scholarship to the CBS-KNAW Fungal Biodiversity Centre. The authors aknowledge support from the Federal Ministery of Education and Research (BMBF) BioFung and the Deutsche Forschungsgemeinschaft (DFG) to GB, ES, and AAB. The work conducted by the U.S. Department of Energy Joint Genome Institute is supported by the Office of Science of the U.S. Department of Energy under Contract No. DE-AC02-05CH11231. FC was supported by the Major Program of National Natural Science Foundation of China (No. 31330059). WC was supported by the National Natural Science Foundation of China (No. 31601446) and the Fundamental Research Funds for the Central Universities (Nos. 2662014BQ051 and 2662015QC003). TB and IB were supported by grants of the Dutch Technology Foundation STW, Applied Science division of NWO, and the Technology Program of the Ministry of Economic Affairs UGC 14270 to RPdV. PAvK, MaA, and DvRU were supported by the Netherlands Technology Foundation STW (LGC 7393). We acknowledge financial support from the FWF (M01693-B22) to DCa.</p><p>This work was in part supported by the Intelligent Synthetic Biology Center of Global Frontier Project (2011-0031955) funded by the Ministry of Education, Science and Technology grants to JHY and Science Foundation Ireland 13/CDA/2142 to OB. NS was supported by a scholarship from the Kurdistan Regional Government of Iraq. HSP was supported by the National Research Foundation of Korea (NRF) grant founded by the Korean Government (no. 2016010945).</p><p>The work at UW-Madison (JHY) was supported by the Intelligent Synthetic Biology Center of Global Frontier Project (2011-0031955) funded by the Ministry of Science, ICT and Future Planning.</p><p>PSD, RH, and RH were supported by the British Mycological Society and the Biotechnology and Biological Sciences Research Council (UK). ES and AAB were supported by CRC 1127 ChemBioSys and CRC-Transregio FungiNet by Deutsche Forschungsgemeinschaft (DFG). JCF was supported by Agilent Technologies (Agilent Thought Leader Award #2871) and the Novo Nordisk Foundation (Grant NNF 13OC0005201). LK was supported by the Hungarian Scientific Research Fund (NN116519) and a Bólyai János Research Fellowship. The sugar transporter analysis was supported by grants AGL2011-29925 and AGL2015-66131- AGL2015-66131-C2-2-R (MINECO/FEDER). BRO was supported by the Irving S. Johnson fund of the Kansas University endowment. We are grateful to FAPESP (The State of São Paulo Research Foundation) for the financial support (2014/06923-6 to FMS; 2012/20549-4 to ARLD; 2011/08945-9 and 2014/11766-7 to JVCO; 2012/19040-0 and 2014/10351-8 to CAU). We are grateful to the Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) and Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) for the financial support (310186/2014-5 and 442333/2014-5 to FMS; 441912/2014-1 to ARLD). We acknowledge the financial support of the Dirección General de Apoyo al Personal Académico, UNAM, projects IN 225710 and IN219813, and The Slovenian Research Agency (P1-0207, P1-0391, and J4-7162). KS was supported by the Slovenian Research Agency (P1-0207) and KS and NK were supported by the Slovenian Research Agency (J4-7162). TCV and MRA acknowledge support from the Villium Foundation, Project VKR023437. GB was supported by a grant from the Deutsche Forschungsgemeinschaft (BR1502/11-2). GB and RF were supported by a grant from the Deutsche Forschungsgemeinschaft (FOR1334/2). AL was supported by St. Petersburg State University, St. Petersburg, Russia (grant no. 15.61.951.2015).</p><p>The Authors thank A Gazdag, R Mohácsi, and LG Tóth (University of Debrecen) for contributing to the experimental work; and V Szabó and T Koszó (University of Debrecen) for the literature search during the construction of FSD and FSRD, respectively. The authors thank C Toft for her help in conducting the phylogenetic analysis of the sugar transporters. The authors thank DG Panaccione for providing the <italic>A. fumigatus easC</italic> mutant strain prior to publication and DR Nelson for naming CYP51 and CYP53 family representatives according to CYP nomenclature. The authors thank Arle Kruckeberg (yeast strain KY73; plasmid pYEX-BX), Barbara Bakker (yeast strain EB.VW4000), Remi Lemoine (yeast strain MaDH4), Jeremy Thorner (yeast strain SEY6210), and Ian Dawes (CMY1050) for kindly providing material used in this study.</p><sec id="FPar9"><title>Availability of data and materials</title><p>The datasets supporting the conclusions of this article are included within the article and its Additional File(s) or available through DDBJ/EMBL/GenBank under the following accessions: <italic>A. aculeatus</italic> ATCC16872 - MRCK00000000, <italic>A. brasiliensis</italic> CBS101740 - LJXV00000000, <italic>A. carbonarius</italic> ITEM5010 - AHIG00000000, <italic>A. foetidus</italic> CBS106.47 - MRBP00000000, <italic>A. glaucus</italic> CBS516.65 - LSTL00000000, <italic>A. sydowii</italic> CBS593.65 - MRCH00000000, <italic>A. tubingensis</italic> CBS134.48 - LJXU00000000, <italic>A. versicolor</italic> CBS583.65 - MRBN00000000, <italic>A. wentii</italic> CBS141173 (DTO134E9) - LJSE00000000, and <italic>A. zonatus</italic> CBS506.65 - MRBM00000000. Links to the raw genome and transcriptome data of these species are available in Additional file <xref rid="MOESM1" ref-type="media">1</xref>D. This also lists the genbank (if available) and JGI accession numbers of the genomes used for comparison as well as the papers in which they have been published. Proteomics data of the wheat bran and sugar beet cultures are available via ProteomeXchange with identifier PXD005563. Proteomics data for the stress experiments are available at <ext-link ext-link-type="uri" xlink:href="http://wwwuser.gwdg.de/~hkusch/GBIO_DeVries/">http://wwwuser.gwdg.de/~hkusch/GBIO_DeVries/</ext-link>.</p></sec><sec id="FPar10"><title>Authors’ contributions</title><p><italic>Genome sequencing and general analysis:</italic> CiC and CYN performed sequencing. Ala, EL, and Ali perfomed transcriptome analysis. HS, KLB, ALa, and AC performed genome assembly. AK, RR, ASa, and IVG performed genome annotation. KB and IVG coordinated the genome sequencing. GCC, GS, and JW facilitated hosting of the genomes in AspGD. JH, RR, and RAS performed phylogenomic analysis and wrote this part of the manuscript. RBT and DA took part in merging and critically reviewing the manuscript. AFL, AG, ASu, GM, and GP collaborated the genome sequencing and preliminary annotation data. <italic>Asexual and sexual reproduction:</italic> PSD coordinated the section. WC, FC, HSP, and JHY performed bioinformatic analysis. NSS, RHa, RHo, and PSD performed bioinformatic analysis and experimental work. PSD and JHY wrote this section of the manuscript. <italic>Primary carbon metabolism:</italic> MRA and BS coordinated the section, analyzed data, and wrote this section of the manuscript. AH, KMO, and PP performed experiments and analyzed the acid production data. LK, EF, MoA, ÁPM, and ES planned and carried out experiments and evaluated data related to alternative oxidases. PMe analyzed genes related to trehalose synthesis. <italic>Plant biomass degradation:</italic> IB and RPdV coordinated this section. BH and MH performed the CAZy analysis of the genomes. ALe, ER, FP, and AT performed bioinformatic analysis and experimental work. AW, GAO, KSH, and MRM performed experimental work. MZ performed the orthology analysis. RPdV wrote this section of the manuscript. <italic>Transporters:</italic> PAvK, MaA, TS, DU, AR, and JV planned and carried out experiments and evaluated data relating to the functional characterization of the 43 A. niger MFS encoding genes. SU and EK performed bioinformatics analysis and wrote the section on nitrate, nitrite, and ammonium transporters. SA, CG, CS, VS, and MF did the bio-informatics, (manual) gene modeling and phylogenetic analyses for the amino acid transporters section, which was written by CS, CG, and SA. GD and CS performed the bioinformatics and phylogenetic analyses for the nucleobase transporters and wrote this section. AR and MS performed the analysis on the urea transporters and wrote this section. MF checked intron-exon organisation of the amino acid, nucleobase and urea transporters. <italic>Secondary metabolism:</italic> AAB, BO, JCF, and ES coordinated the section. ESh designed and performed bioinformatics analyses. ESh and JCF compared and analyzed bioinformatic and experimental evidence. NK, KS, and GA performed bioinformatic and experimental work for cytochromes P450 and aegerolysin-like proteins. AG, ASu, and GP contribute to mycotoxins biosynthetic cluster annotation in black aspergilli. All authors contributed to discussions and wrote this section of the manuscript. <italic>Stress response:</italic> EO, VR, NvdW, MZ, ZK, and MM constructed the FSDatabase and FSRDatabase. HK, SABS, SF, ÖB, GHB, AFJR, ELL, JPO, VM, NM, MM, DCa, SR, JR, RF, GB, EO, MM, TE, RPdV, and IP performed genome comparison, phylogeny, evolutionary analysis, design of experiments, and interpretation of data. HK, SF, EL, JPO, NM, SR, JR, and EO carried out experiments. HK, SABS, SF, and GHB performed proteome analysis. HK, SABS, DC, VM, GHB, IP, and MM wrote this section of the manuscript. <italic>Signal transduction:</italic> CAU, CaC, RACdS, ARLD, IM, DMRP, Rru, FMS, JVCO, and GHG analyzed the signal transduction pathways. This section was written by GHG. <italic>DNA binding proteins:</italic> CS, MF, and LH did the bio-informatics, (manual) gene modeling and phylogenetic analyses of the DNA binding proteins, and wrote this section. <italic>Project leaders:</italic> RPdV, PSD, PAvK, JW, SB, and IVG. RPdV coordinated the project. RPdV and PSD merged the manuscript. 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