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Schoepp-Cothenet, B. et al. The ineluctable claim for the trans-iron elements molybdenum and/or tungsten in the agent of life. Sci. Rep. 2, 263 (2012).
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Nitschke, W. & Russell, M. J. Beating the acetyl coenzyme A-pathway to the agent of life. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 368, 20120258 (2013).
Schoepp-Cothenet, B. et al. On the accepted amount of bioenergetics. Biochim. Biophys. Acta 1827, 79–93 (2013).
Sousa, F. L. et al. Early bioenergetic evolution. Philos. Trans. R. Soc. Lond. B Biol. Sci. 368, 20130088 (2013).
Grimaldi, S., Schoepp-Cothenet, B., Ceccaldi, P., Guigliarelli, B. & Magalon, A. The prokaryotic Mo/W-bisPGD enzymes family: A catalytic crammer in bioenergetic. Biochim. Biophys. Acta 1827, 1048–1085 (2013).
Abin, C. A. & Hollibaugh, J. T. Transcriptional acknowledgment of the astrict anaerobe Desulfuribacillus stibiiarsenatis MLFW-2T to advance on antimonate and added terminal electron acceptors. Environ. Microbiol. 21, 618–630 (2019).
Shi, L.-D. et al. Multi-omics acknowledge assorted abeyant antimonate reductases from phylogenetically assorted microorganisms. Appl. Microbiol. Biotechnol. 103, 9119–9129 (2019).
Bilous, P. T., Cole, S. T., Anderson, W. F. & Weiner, J. H. Nucleotide arrangement of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli. Mol. Microbiol. 2, 785–795 (1988).
Weiner, J. H., MacIsaac, D. P., Bishop, R. E. & Bilous, P. T. Purification and backdrop of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzyme with ample substrate specificity. J. Bacteriol. 170, 1505–1510 (1988).
Cammack, R. & Weiner, J. H. Electron paramagnetic resonance spectroscopic assuming of dimethyl sulfoxide reductase of Escherichia coli. Biochemistry 29, 8410–8416 (1990).
Schindelin, H., Kisker, C., Hilton, J., Rajagopalan, K. V. & Rees, D. C. Clear anatomy of DMSO reductase: Redox-linked changes in molybdopterin coordination. Science 272, 1615–1621 (1996).
Schneider, F. et al. Clear anatomy of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Å resolution. J. Mol. Biol. 263, 53–69 (1996).
Rothery, R. A., Workun, G. J. & Weiner, J. H. The prokaryotic circuitous iron–sulfur molybdoenzyme family. Biochim. Biophys. Acta 1778, 1897–1929 (2008).
Hille, R., Hall, J. & Basu, P. The mononuclear molybdenum enzymes. Chem. Rev. 114, 3963–4038 (2014).
McEwan, A. G., Ridge, J. P., McDevitt, C. A. & Hugenholtz, P. The DMSO reductase ancestors of microbial molybdenum enzymes: Molecular backdrop and role in the dissimilatory abridgement of baneful elements. Geomicrobiol. J. 19, 3–21 (2002).
Sparacino-Watkins, C., Stolz, J. F. & Basu, P. Nitrate and periplasmic nitrate reductases. Chem. Soc. Rev. 43, 676–706 (2014).
Sforna, M. C. et al. Evidence for arsenic metabolism and cycling by microorganisms 2.7 billion years ago. Nat. Geosci. 7, 811–815 (2014).
Stolz, J. F., Basu, P., Santini, J. M. & Oremland, R. S. Arsenic and selenium in microbial metabolism. Annu. Rev. Microbiol. 60, 107–130 (2006).
Zargar, K., Hoeft, S., Oremland, R. & Saltikov, C. W. Identification of a atypical arsenite oxidase gene, arxA, in the haloalkaliphilic, arsenite-oxidizing bacillus Alkalilimnicola ehrlichii ache MLHE-1. J. Bacteriol. 192, 3755–3762 (2010).
Zargar, K. et al. ArxA, a new clade of arsenite oxidase aural the DMSO reductase ancestors of molybdenum oxidoreductases. Environ. Microbiol. 14, 1635–1645 (2012).
Kulp, T. R. et al. Arsenic(III) fuels anoxygenic photosynthesis in hot bounce biofilms from Mono Lake California. Science 321, 967–970 (2008).
Stolz, J. F. Gaia and her microbiome. FEMS Microbiol. Ecol. 93, flw247 (2017).
Oremland, R. S., Saltikov, C. W., Wolfe-Simon, F. & Stolz, J. F. Arsenic in the change of Earth and exoteric ecosystems. Geomicrobiol. J. 26, 522–536 (2009).
Lebrun, E. et al. Arsenite oxidase, an age-old bioenergetic enzyme. Mol. Biol. Evol. 20, 686–693 (2003).
Duval, S., Ducluzeau, A.-L., Nitschke, W. & Schoepp-Cothenet, B. Agitator phylogenies as markers for the blaze accompaniment of the environment: The case of respiratory arsenate reductase and accompanying enzymes. BMC Evol. Biol. 8, 206 (2008).
van Lis, R., Nitschke, W., Duval, S. & Schoepp-Cothenet, B. Arsenics as bioenergetic substrates. Biochim. Biophys. Acta 1827, 176–188 (2013).
Ducluzeau, A.-L. et al. Was nitric oxide the aboriginal abysmal electron sink?. Trends Biochem. Sci. 34, 9–15 (2009).
Harel, A., Häggblom, M. M., Falkowski, P. G. & Yee, N. Change of prokaryotic respiratory molybdoenzymes and the abundance of their genomic co-occurrence. FEMS Microbiol. Ecol. 92, 187 (2016).
Edwardson, C. F. & Hollibaugh, J. T. Metatranscriptomic assay of prokaryotic communities alive in sulfur and arsenic cycling in Mono Lake, California, USA. ISME J. 11, 2195–2208 (2017).
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Huelsenbeck, J. P., Ronquist, F., Nielsen, R. & Bollback, J. P. Bayesian inference of phylogeny and its appulse on evolutionary biology. Science 294, 2310–2314 (2001).
Huelsenbeck, J. P. & Crandall, K. A. Phylogeny admiration and antecedent testing application best likelihood. Annu. Rev. Ecol. Syst. 28, 437–466 (1997).
Weiss, M. C. et al. The assay and abode of the aftermost accepted accepted ancestor. Nat. Microbiol. 1, 16116 (2016).
Wu, D. et al. A phylogeny-driven genomic encyclopaedia of Bacilli and Archaea. Nature 462, 1056–1060 (2009).
Mukherjee, S. et al. 1,003 advertence genomes of bacterial and archaeal isolates aggrandize advantage of the timberline of life. Nat. Biotechnol. 35, 676–683 (2017).
Krafft, T. et al. Cloning and nucleotide arrangement of the psrA gene of Wolinella succinogenes polysulphide reductase. Eur. J. Biochem. 206, 503–510 (1992).
Heinzinger, N. K., Fujimoto, S. Y., Clark, M. A., Moreno, M. S. & Barrett, E. L. Arrangement assay of the phs operon in Salmonella typhimurium and the addition of thiosulfate abridgement to anaerobic activity metabolism. J. Bacteriol. 177, 2813–2820 (1995).
Wells, M. et al. Respiratory selenite reductase from Bacillus selenitireducens ache MLS10. J. Bacteriol. 201, e00614-e618 (2019).
Hensel, M., Hinsley, A. P., Nikolaus, T., Sawers, G. & Berks, B. C. The abiogenetic base of tetrathionate respiration in Salmonella typhimurium. Mol. Microbiol. 32, 275–287 (1999).
Kuroda, M. et al. Molecular cloning and assuming of the srdBCA operon, encoding the respiratory selenate reductase complex, from the selenate-reducing bacillus Bacillus selenatarsenatis SF-1. J. Bacteriol. 193, 2141–2148 (2011).
Cozen, A. E. et al. Transcriptional map of respiratory versatility in the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. J. Bacteriol. 191, 782–794 (2009).
Stamatakis, A. RAxML adaptation 8: A apparatus for phylogenetic assay and post-analysis of ample phylogenies. Bioinformatics 30, 1312–1313 (2014).
Wagner, T., Ermler, U. & Shima, S. The methanogenic CO2 reducing-and-fixing agitator is bifunctional and contains 46 [4Fe–4S] clusters. Science 354, 114–117 (2016).
Sawers, G. The hydrogenases and formate dehydrogenases of Escherichia coli. Antonie Van Leeuwenhoek 66, 57–88 (1994).
Jormakka, M., Törnroth, S., Byrne, B. & Iwata, S. Molecular base of proton motive force generation: Anatomy of formate dehydrogenase-N. Science 295, 1863–1868 (2002).
Raaijmakers, H. et al. Gene arrangement and the 1.8 Å clear anatomy of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas. Anatomy 10, 1261–1272 (2002).
Boyington, J. C., Gladyshev, V. N., Khangulov, S. V., Stadtman, T. C. & Sun, P. D. Clear anatomy of formate dehydrogenase H: Catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. Science 275, 1305–1308 (1997).
Khangulov, S. V., Gladyshev, V. N., Dismukes, G. C. & Stadtman, T. C. Selenium-containing formate dehydrogenase H from Escherichia coli: A molybdopterin agitator that catalyzes formate blaze after oxygen transfer. Biochemistry 37, 3518–3528 (1998).
Oh, J. I. & Bowien, B. Structural assay of the fds operon encoding the NAD -linked formate dehydrogenase of Ralstonia eutropha. J. Biol. Chem. 273, 26349–26360 (1998).
Niks, D., Duvvuru, J., Escalona, M. & Hille, R. Spectroscopic and alive backdrop of the molybdenum-containing, NAD -dependent formate dehydrogenase from Ralstonia eutropha. J. Biol. Chem. 291, 1162–1174 (2016).
Yu, X., Niks, D., Mulchandani, A. & Hille, R. Efficient abridgement of CO2 by the molybdenum-containing formate dehydrogenase from Cupriavidus necator (Ralstonia eutropha). J. Biol. Chem. 292, 16872–16879 (2017).
Stock, T. & Rother, M. Selenoproteins in Archaea and Gram-positive bacteria. Biochim. Biophys. Acta 1790, 1520–1532 (2009).
Luque-Almagro, V. M. et al. Bacterial nitrate assimilation: Gene administration and regulation. Biochem. Soc. Trans. 39, 1838–1843 (2011).
Catling, D. C. & Zahnle, K. J. The Archean atmosphere. Sci. Adv. 6, eaax1420 (2020).
Glaser, P., Danchin, A., Kunst, F., Zuber, P. & Nakano, M. M. Identification and abreast of a gene appropriate for nitrate assimilation and anaerobic advance of Bacillus subtilis. J. Bacteriol. 177, 1112–1115 (1995).
Martínez-Espinosa, R. M., Marhuenda-Egea, F. C. & Bonete, M. J. Assimilatory nitrate reductase from the haloarchaeon Haloferax mediterranei: Purification and characterisation. FEMS Microbiol. Lett. 204, 381–385 (2001).
Kilic, V., Kilic, G. A., Kutlu, H. M. & Martínez-Espinosa, R. M. Nitrate abridgement in Haloferax alexandrinus: The case of assimilatory nitrate reductase. Extremophiles 21, 551–561 (2017).
Ruiz, B. et al. The nitrate assimilatory alleyway in Sinorhizobium meliloti: Addition to NO production. Front. Microbiol. 10, 1526 (2019).
Hidalgo-García, A. et al. Rhizobium etli produces nitrous oxide by coupling the assimilatory and denitrification pathways. Front. Microbiol. 10, 980 (2019).
Flores, E., Frías, J. E., Rubio, L. M. & Herrero, A. Photosynthetic nitrate assimilation in cyanobacteria. Photosyn. Res. 83, 117–133 (2005).
Ordoñez, O. F., Rasuk, M. C., Soria, M. N., Contreras, M. & Farías, M. E. Haloarchaea from the Andean Puna: Biological role in the activity metabolism of arsenic. Microb. Ecol. 76, 695–705 (2018).
Härtig, C. et al. Chemolithotrophic advance of the aerobic hyperthermophilic bacillus Thermocrinis ruber OC 14/7/2 on monothioarsenate and arsenite. FEMS Microbiol. Ecol. 90, 747–760 (2014).
Svetlitshnyi, V., Rainey, F. & Wiegel, J. Thermosyntropha lipolytica gen. nov., sp. nov., a lipolytic, anaerobic, alkalitolerant, thermophilic bacillus utilizing short- and long-chain blubbery acids in syntrophic coculture with a methanogenic archaeum. Int. J. Syst. Bacteriol. 46, 1131–1137 (1996).
Martin, W., Baross, J., Kelley, D. & Russell, M. J. Hydrothermal vents and the agent of life. Nat. Rev. Microbiol. 6, 805–814 (2008).
Bult, C. J. et al. Complete genome arrangement of the methanogenic archaeon, Methanococcus jannaschii. Science 273, 1058–1073 (1996).
Slesarev, A. I. et al. The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens. Proc. Natl. Acad. Sci. USA 99, 4644–4649 (2002).
Hendrickson, E. L. et al. Complete genome arrangement of the genetically acquiescent hydrogenotrophic methanogen Methanococcus maripaludis. J. Bacteriol. 186, 6956–6969 (2004).
Andreesen, J. R. & Ljungdahl, L. G. Nicotinamide adenine dinucleotide phosphate-dependent formate dehydrogenase from Clostridium thermoaceticum: Purification and properties. J. Bacteriol. 120, 6–14 (1974).
Graentzdoerffer, A., Rauh, D., Pich, A. & Andreesen, J. R. Molecular and biochemical assuming of two tungsten- and selenium-containing formate dehydrogenases from Eubacterium acidaminophilum that are associated with apparatus of an iron-only hydrogenase. Arch. Microbiol. 179, 116–130 (2003).
Jones, J. B., Dilworth, G. L. & Stadtman, T. C. Occurrence of selenocysteine in the selenium-dependent formate dehydrogenase of Methanococcus vannielii. Arch. Biochem. Biophys. 195, 255–260 (1979).
Wood, G. E., Haydock, A. K. & Leigh, J. A. Action and adjustment of the formate dehydrogenase genes of the methanogenic archaeon Methanococcus maripaludis. J. Bacteriol. 185, 2548–2554 (2003).
Costa, C., Teixeira, M., LeGall, J., Moura, J. J. G. & Moura, I. Formate dehydrogenase from Desulfovibrio desulfuricans ATCC 27774: Abreast and spectroscopic assuming of the alive sites (heme, iron-sulfur centers and molybdenum). JBIC 2, 198–208 (1997).
Zhang, Y., Romero, H., Salinas, G. & Gladyshev, V. N. Dynamic change of selenocysteine appliance in bacteria: A antithesis amid selenoprotein accident and change of selenocysteine from redox alive cysteine residues. Genome Biol. 7, R94 (2006).
Rother, M. & Krzycki, J. A. Selenocysteine, pyrrolysine, and the different activity metabolism of methanogenic Archaea. Archaea 2010, 453642 (2010).
Peng, T., Lin, J., Xu, Y.-Z. & Zhang, Y. Comparative genomics reveals new evolutionary and ecological patterns of selenium appliance in bacteria. ISME J. 10, 2048–2059 (2016).
Mariotti, M. et al. Change of selenophosphate synthetases: Emergence and alteration of action through absolute duplications and alternate subfunctionalization. Genome Res. 25, 1256–1267 (2015).
Ogawa, K. et al. The nasB operon and nasA gene are appropriate for nitrate/nitrite assimilation in Bacillus subtilis. J. Bacteriol. 177, 1409–1413 (1995).
Suzuki, I., Sugiyama, T. & Omata, T. Primary anatomy and transcriptional adjustment of the gene for nitrite reductase from the cyanobacterium Synechococcus PCC 7942. Plant Cell Physiol. 34, 1311–1320 (1993).
Gangeswaran, R., Lowe, D. J. & Eady, R. R. Purification and assuming of the assimilatory nitrate reductase of Azotobacter vinelandii. Biochem. J. 289(Pt 2), 335–342 (1993).
Rubio, L. M., Flores, E. & Herrero, A. Purification, cofactor analysis, and site-directed mutagenesis of Synechococcus ferredoxin-nitrate reductase. Photosyn. Res. 72, 13–26 (2002).
Lin, J. T., Goldman, B. S. & Stewart, V. Structures of genes nasA and nasB, encoding assimilatory nitrate and nitrite reductases in Klebsiella pneumoniae M5al. J. Bacteriol. 175, 2370–2378 (1993).
Blasco, R., Castillo, F. & Martínez-Luque, M. The assimilatory nitrate reductase from the phototrophic bacterium, Rhodobacter capsulatus E1F1, is a flavoprotein. FEBS Lett. 414, 45–49 (1997).
Krafft, T. & Macy, J. M. Purification and assuming of the respiratory arsenate reductase of Chrysiogenes arsenatis. Eur. J. Biochem. 255, 647–653 (1998).
Afkar, E. et al. The respiratory arsenate reductase from Bacillus selenitireducens ache MLS10. FEMS Microbiol. Lett. 226, 107–112 (2003).
Ellis, P. J., Conrads, T., Hille, R. & Kuhn, P. Clear anatomy of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two clear forms at 1.64 Å and 2.03 Å. Anatomy 9, 125–132 (2001).
Warelow, T. P., Pushie, M. J., Cotelesage, J. J. H., Santini, J. M. & George, G. N. The alive armpit anatomy and catalytic apparatus of arsenite oxidase. Sci. Rep. 7, 1757 (2017).
Karrasch, M., Börner, G. & Thauer, R. K. The molybdenum cofactor of formylmethanofuran dehydrogenase from Methanosarcina barkeri is a molybdopterin guanine dinucleotide. FEBS Lett. 274, 48–52 (1990).
Schmitz, R. A., Albracht, S. P. & Thauer, R. K. A molybdenum and a tungsten isoenzyme of formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei. Eur. J. Biochem. 209, 1013–1018 (1992).
Yamamoto, I., Saiki, T., Liu, S. M. & Ljungdahl, L. G. Purification and backdrop of NADP-dependent formate dehydrogenase from Clostridium thermoaceticum, a tungsten-selenium-iron protein. J. Biol. Chem. 258, 1826–1832 (1983).
Jones, J. B. & Stadtman, T. C. Selenium-dependent and selenium-independent formate dehydrogenases of Methanococcus vannielii. Separation of the two forms and assuming of the antiseptic selenium-independent form. J. Biol. Chem. 256, 656–663 (1981).
Boratyn, G. M. et al. Domain added lookup time accelerated BLAST. Biol. Direct 7, 12 (2012).
Markowitz, V. M. et al. The chip microbial genomes (IMG) system. Nucl. Acids Res. 34, D344–D348 (2006).
Bertero, M. G. et al. Insights into the respiratory electron alteration alleyway from the anatomy of nitrate reductase A. Nat. Struct. Biol. 10, 681–687 (2003).
Afshar, S., Johnson, E., de Vries, S. & Schröder, I. Backdrop of a thermostable nitrate reductase from the hyperthermophilic archaeon Pyrobaculum aerophilum. J. Bacteriol. 183, 5491–5495 (2001).
Ramírez-Arcos, S., Fernández-Herrero, L. A. & Berenguer, J. A thermophilic nitrate reductase is amenable for the ache specific anaerobic advance of Thermus thermophilus HB8. Biochim. Biophys. Acta 1396, 215–227 (1998).
Thorell, H. D., Stenklo, K., Karlsson, J. & Nilsson, T. A gene array for chlorate metabolism in Ideonella dechloratans. Appl. Environ. Microbiol. 69, 5585–5592 (2003).
Schröder, I., Rech, S., Krafft, T. & Macy, J. M. Purification and assuming of the selenate reductase from Thauera selenatis. J. Biol. Chem. 272, 23765–23768 (1997).
McDevitt, C. A., Hugenholtz, P., Hanson, G. R. & McEwan, A. G. Molecular assay of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: Its abode in the dimethyl sulphoxide reductase ancestors of microbial molybdopterin-containing enzymes. Mol. Microbiol. 44, 1575–1587 (2002).
Méjean, V. et al. TMAO anaerobic respiration in Escherichia coli: Involvement of the tor operon. Mol. Microbiol. 11, 1169–1179 (1994).
Czjzek, M. et al. Clear anatomy of breakable trimethylamine N-oxide reductase from Shewanella massilia at 2.5 Å resolution. J. Mol. Biol. 284, 435–447 (1998).
Pierson, D. E. & Campbell, A. Cloning and nucleotide arrangement of bisC, the structural gene for biotin sulfoxide reductase in Escherichia coli. J. Bacteriol. 172, 2194–2198 (1990).
White, H., Strobl, G., Feicht, R. & Simon, H. Carboxylic acerbic reductase: A new tungsten agitator catalyses the abridgement of non-activated carboxylic acids to aldehydes. Eur. J. Biochem. 184, 89–96 (1989).
Mukund, S. & Adams, M. W. The atypical tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its accord in a different glycolytic pathway. J. Biol. Chem. 266, 14208–14216 (1991).
Hu, Y., Faham, S., Roy, R., Adams, M. W. W. & Rees, D. C. Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: The 1.85 Å resolution clear anatomy and its mechanistic implications. J. Mol. Biol. 286, 899–914 (1999).
Mukund, S. & Adams, M. W. Assuming of a atypical tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon, Thermococcus litoralis. A role for tungsten in peptide catabolism. J. Biol. Chem. 268, 13592–13600 (1993).
Mukund, S. & Adams, M. W. Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a atypical tungsten-containing agitator with a abeyant glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 270, 8389–8392 (1995).
Park, M.-O., Mizutani, T. & Jones, P. R. Glyceraldehyde-3-phosphate ferredoxin oxidoreductase from Methanococcus maripaludis. J. Bacteriol. 189, 7281–7289 (2007).
Reher, M., Gebhard, S. & Schönheit, P. Glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) and nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN), key enzymes of the corresponding adapted Embden–Meyerhof pathways in the hyperthermophilic crenarchaeota Pyrobaculum aerophilum and Aeropyrum pernix. FEMS Microbiol. Lett. 273, 196–205 (2007).
Vorholt, J. A., Vaupel, M. & Thauer, R. K. A selenium-dependent and a selenium-independent formylmethanofuran dehydrogenase and their transcriptional adjustment in the hyperthermophilic Methanopyrus kandleri. Mol. Microbiol. 23, 1033–1042 (1997).
Nakamura, T., Yamada, K. D., Tomii, K. & Katoh, K. Parallelization of MAFFT for all-embracing assorted arrangement alignments. Bioinformatics 34, 2490–2492 (2018).
Capella-Gutiérrez, S., Silla-Martínez, J. M. & Gabaldón, T. trimAl: A apparatus for automatic alignment accent in all-embracing phylogenetic analyses. Bioinformatics 25, 1972–1973 (2009).
Kalyaanamoorthy, S., Minh, B. Q., Wong, T. K. F., von Haeseler, A. & Jermiin, L. S. ModelFinder: Fast archetypal alternative for authentic phylogenetic estimates. Nat. Methods 14, 587–589 (2017).
Le, S. Q., Dang, C. C. & Gascuel, O. Modeling protein change with several amino acerbic backup matrices depending on armpit rates. Mol. Biol. Evol. 29, 2921–2936 (2012).
Miller, M. A., Pfeiffer, W. & Schwartz, T. Creating the CIPRES Science Gateway for inference of ample phylogenetic trees. In 2010 Gateway Computing Environments Workshop (GCE) 1–8 (2010). https://doi.org/10.1109/GCE.2010.5676129.
Letunic, I. & Bork, P. Interactive Timberline of Activity (iTOL) v4: Recent updates and new developments. Nucleic Acids Res. 47, W256–W259 (2019).
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