Posted on Authorea 19 Nov 2020 — The copyright holder is the author/funder. All rights reserved. No reuse without permission. — https://doi.org/10.22541/au.160577285.57603701/v1 — This a preprint and has not been peer reviewed. Data may be preliminary. eerh usa cdm fSine,Pscio ocwRgo,Rsi.Emi:[email protected] Protein E-mail: of Russia. Institute Region, Proteomics, Moscow Pushchino, and Sciences, Bioinformatics of of Academy Russian Laboratory Research, Galzitskaya, Oxana to: *Correspondence Russia Russia. Region, Region, Moscow Moscow Pushchino, 142290, Sciences, of Academy 4 Russian Sciences”, Research, of Protein Academy of Russian Institute the Russia of Region, Research Federal Moscow Biological Sciences, Pushchino, for of 142290, Center Academy Russian Scientific Microorganisms, ”Pushchino Russia of Center Region, Physiology Research Moscow and Pushchino, Biochemistry of 142290, Institute Sciences”, Skryabin of Academy Russian the of Research 1 evolution Deryusheva I. proteins Evgeniya S1 ribosomal proteins Bacterial S1 ribosomal title: bacterial Running of analysis be can evolutionary which and server, the Sequence into ribosomal integrated bacterial are of data dN/dS development presented as evolutionary to The well the useful repeat. as that be single motifs, http://oka.protres.ru:4200. suggested can to phyla; at logo data assemblies data accessed different and research multiple structured the composition obtained from 24 and evolved acid The is in collected S1 amino work identified The protein. identity, proteins this S1 percent were proteins. knowledge, determining bacterial that S1 for our in sequences ribosomal To resource ratio bacterial S1 a evolution. of as 1333 to the history during biologists of assembles of evolutionary computer form of analysis the one independently/dependently a repeats of for comparative can multiple domain. from study evidence this phyla from provide first globular sense In such will a repeats: classical how phyla into structural versa. the demonstrate bacterial with folded vice we in the proteins is or for differs of repeat relationships development repeats, proteins each evolutionary evolutionary single S1 of where subunit, the study ribosomal of 30S organization, the theories the of “bead-on-string” data, proposed of family a recent protein The has our ribosomal on and important Based proteins. repeats functionally and tandem most mRNA with and protein largest both the with is interacts protein which S1 bacterial multi-domain The Abstract 2020 19, November 4 Sciences” of Academy 3 Russian the of Research 2 Biological for Center 1 Deryusheva Evgenia S1 ribosomal bacterial proteins of analysis evolutionary and Sequence nttt fTertcladEprmna ipyis usa cdm fSine,129,Pushchino, 142290, Sciences, of Academy Russian Biophysics, Experimental and Theoretical of Institute nttt fPoenRsac,RsinAaeyo Sciences of Research Academy Protein Russian of Research, Institute Sciences Protein of of Academy Institute Russian 3 Instrumentation, Biological for Scientific Institute ”Pushchino Center Research Federal Instrumentation, Biological for Institute nttt o ilgclIsrmnain eea eerhCne PscioSinicCne o Biological for Center Scientific ”Pushchino Center Research Federal Instrumentation, Biological for Institute 1 1 nryV Machulin V. Andrey , nryMachulin Andrey , 2 2 ai .Matyunin A. Maxim , ai Matyunin Maxim , 1 3 3 n xn Galzitskaya Oxana and , n xn .Galzitskaya V. Oxana and 3,4* 4 Posted on Authorea 19 Nov 2020 — The copyright holder is the author/funder. All rights reserved. No reuse without permission. — https://doi.org/10.22541/au.160577285.57603701/v1 — This a preprint and has not been peer reviewed. Data may be preliminary. ehv eetysonta h ubro oan nS sadsiciecaatrsi ftephylogenetic the of characteristic distinctive a is which S1 between in differences domains the of mycobacteria, number the of that types rDNA. shown 8 recently 16S have main of We analysis the the for 273 ribosomal in biomarker the of revealed a Of not family as were the bacteria. S1 in Gram-negative identified domains protein and were S1 Gram-positive ribosomal phyla of between 12 alignment relationship sequences, pairwise the al. 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Posted on Authorea 19 Nov 2020 — The copyright holder is the author/funder. All rights reserved. No reuse without permission. — https://doi.org/10.22541/au.160577285.57603701/v1 — This a preprint and has not been peer reviewed. Data may be preliminary. eut n discussion at and accessed Results be can server S1 ( The program browser. database cross-platform ( document-oriented language a as ( used framework was web Flask the used We sequence. protein a in acids development amino of Web number the count to were used was described logos Bio.SeqUtils.ProtParam.ProteinAnalysis as sequence calculated func- model was The Bio.pairwise2.align.globalds Yang PID the using (Biopython).The program. aligned matrix was this in Bio.SubsMat.MatrixInfo.blosum62 sequences of the acid with amino parameters ( of tion ( standard pair server service each the 3 identity), MEGA WebLogo used quence the the we by by work, created implemented our In was (ClustalW). 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Chlamydia 39 , Posted on Authorea 19 Nov 2020 — The copyright holder is the author/funder. All rights reserved. No reuse without permission. — https://doi.org/10.22541/au.160577285.57603701/v1 — This a preprint and has not been peer reviewed. 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Posted on Authorea 19 Nov 2020 — The copyright holder is the author/funder. All rights reserved. No reuse without permission. — https://doi.org/10.22541/au.160577285.57603701/v1 — This a preprint and has not been peer reviewed. Data may be preliminary. tidadfut oan)apast evtlfrteatvt n ucinlt fteepoen.This proteins. proteins these of of part functionality central and the activity Thus, this the of site. for uniqueness binding vital the RNA confirms be strongest again to the once appears as which domains) R68, it and fourth consider ( N64, and to PNPase H34, from Mollicutes) (third us L22, (Tenericutes, domain allows proteins F19, S1 and domain the residues: among repeat single with (68%) five S1 identity identity by highest from highest sufficient formed the domains the is is has S1 has (six) group the domain domain this and in this S1 domain ) addition, the third In of 2001). The al., repeats domains. functions. et of other necessary (Andrade number the maximum repeats all the several perform its proteins, to of both of chain bacterial formed exception investigated one are the the from which For and with repeats, multiple repeats homologue, homologous single modern of with its examples oligomers of are from structure there However, repeating character. intrachain activitymulti-chain contained the functional necessarily reflect effective which may for ancestor, ancestor homo-oligomers common formed a that and from evolved repeat, repeat each repeats repeat for These functions single corresponding unclear. a the proteins still repeats, S1 is protein of evolution ribosomal nature their 30S the understanding bacterial of of problem The family the overall of development the evolutionary for Possible important percentage more low obviously rather is a the domain) reveals Discussion that (S1 Note group scaffold each domain. proteins S1 structure in these the of the domains of functioning amino individual that conservatism different the the indicating of identity, with between percentage associated of sequences domain the is structural the domains, which S1 explained six of same, the is and the alignment in K four almost region containing and is flexible E proteins residues a residues S1 acid as ‘disorder-promoting’ of well phyla of representative as predominance terminus, most The and domain. linkers S1 flexible the by of structure the in structural for and in specific W) represented acids F, is (Y, which amino domain, residues of S1 the tendencies is proteins position-specific S1 ribosomal of Amino unit a (Analysis structural by domains) basic the structural of above, of percentage mentioned number As the the calculated with and accordance collected (in we group composition, proteins, each acid S1 for ribosomal residues acid bacterial amino of sequences available all For gives composition unfortunately, acid ratio, interpret. dN/dS Amino to the (dN/dS difficult of selection analysis are phyla), negative that bacteria only results (dN/dS between ambiguous phyla) and selection for (within between negative domains proteins, and phyla) S1 S1 individual (within between four-domain proteins and the S1 (within example, For six-domain proteins (for S1 revealed group. was four-domain this selection the in positive 1.05: relatively sequence a = acid Actinobacteria, dN/dS nucleic phylum the the of of representatives some pairs all of characteristic (dN/dS selection phylum the negative for nexilis proteins, found S1 was two-domain (0.75) For and ratio dN/dS Tenericutes. high = phylum relatively (dN/dS < the specific a Proteobacteria Also, to a phylum relative 1.26). the species) example: to = Bacteroidetes relative (for all (dN/dS Tenericutes revealed protein not was and the selection 1.46) but positive of (some, Actinobacteria, region phylum phylogeny (dN/dS certain the of a selection branch negative in one only proteins, within observed and/or usually is domain) selection such because )as rdmnts eaieyhg Nd aiswr on for found were ratios dN/dS high Relatively predominates. also 1) ciolnsfriuliensis Actinoplanes β- Poebcei) o he-oanadfiedmi 1poen,ngtv eeto (dN/dS selection negative proteins, S1 five-domain and three-domain For (Proteobacteria). arlwt nadditional an with barrel hdccu wratislaviensis Rhodococcus 50 http://oka.protres.ru:4200 oeatossgetdta h omnacso ftefml a nedasingle a indeed was family the of ancestor common the that suggested authors Some . β- tad nrbsmlpoen 1 n r hrceitc fa additional an of characteristics are L and A S1. proteins ribosomal in strands β- rnhdaioais(,V ) scnb enfo al ,V ,FadTare T and F I, V, 2, Table from seen be can As I). 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No reuse without permission. — https://doi.org/10.22541/au.160577285.57603701/v1 — This a preprint and has not been peer reviewed. Data may be preliminary. hlmBceodts ln ihPoebcei,Friue,adAtnbcei,aeas mn h most the among also rhizosphere are the Actinobacteria, in and groups Firmicutes, bacterial four, Proteobacteria, common one, with 4). has along (Figure Bacteroidetes, Cytophagia Bacteroidetes Phylum class phylum The the Gemmatimonadates, within phyla). the domains for Bacteroidia number six class (constant and domains ribosomal and S1 the this Chlorobi six that contains show Fibrobacteres, in always data almost Ignavibacteriae, Our Ignavibacteriae group this group. and in ancient protein more Gemmatimonadates Chlorobi, S1 phylogenetically phyla a Fibrobacteres, considered phyla the is member Fibrobacteres include phylum main also the after authors named group Some bacteria of Bacteroidetes. superphylum of a and organisms most is group and of FCB largest genome The the the is data, PVC, other published superphylum each some of to to is phyla closer have changes According other proteins evolutionary can with to 4). some Planctomycetes comparison susceptible (Figure while in in domains Planctomycetes, domains, indels phylum S1 S1 clan conserved the six six PVC characteristic and contain the five, and generally in four, Chlamydiae phyla rRNA Verrucomicrobia, Verrucomicrobia Planctomycetes, 16S and phyla of Chlamydiae the analysis group to the ancientused above, phylogenetically a mentioned in considered domains As is S1 literature microorganisms structural the of in of group Spirochaetes number distinct phylum constant and the the Moreover, evolutionary in bacteria. The Nitrospi- reflected these Spirochaetes, domains. apparently lifestyles Fusobacteria, S1 is Deferribacteres, copiotrophic six Nitrospinae/Tectomicrobia Caldiserica, have a as rae, Alphaproteobacteria with phyla class such associated the of were development and independent Acidobacteria phyla phyla these and Alphaproteobacteria the with to Aquificae data, associated phylum our belonging be of the bacteria representatives to from of both considered development bacteria that often evolutionary gene data, is The horizontal phylum our frequent domains. Acidobacteria to to S1 the due According six phyla is strictly niches. have two closeness inorganic Epsilonproteobacteria ecological This the class in common Proteobacteria. of to signature to species the due related indel the of closely transfer conserved are relationship in the Aquificae specific found by that The uniquely gested supported comparison is changes. in is domains insignificantly which Epsilonproteobacteria Actinobacteria, S1 or pyrophosphatase, the the of constantly to number to number the Aquificae addition this in phylum (in where diversity Proteobacteria phyla, greatest within other the classes have with these phyla) of numbers Firmicutes data, different and our having Bacteriodites to Deltaproteobacteria Gamma-proteobacteria According and as Beta-proteobacteria domains. time with S1 domains, same six the and five at have Bacteria out of branched phyla other Alphaproteobacteria that most suggest than proteins various later Proteobacteria of out with analyses branched Phylogenetic along Gamma-proteobacteria 4). and (Figure Beta-proteobacteria domains a that S1 evolu- up structural are of make number Betaproteobacteria they constant together six. and to Gamma-proteobacteria Acidithiobacillia, the one and this from Chromatibacteria Gamma-proteobacteria in ranges called to class taxon domains oldest related the S1 closely be of most to number tionary considered Deltaproteobacteria the is 4). and Epsilonproteobacteria phy- proteobacteria, (Figure – that this, Gamma domains Note Alpha Within S1 domains. domains, structural S1 1b). S1 six phylum and (Figure or six sequences S1 five have of of proteins number Epsilonproteobacteria consist all different and of a Acidithiobacillia 55% by Thus, represented of the are consists of efficiency classes Proteobacteria the logenetic the only above, reduces protein mentioned the S1 As functionality of the N-terminus its of the not repeats from but domains six functions, S1 with from protein two proteins S1 or well-studied protein C-terminus the ribosomal the of 30S from bacterial One the data. is experimental domain with consistent is suggestion 27 tsol entd htteepyao hlgntctesaeotna h aelvl hl the while level, same the at often are trees phylogenetic on phyla these that noted, be should It . 29,52 h lgflxacasi hrceie ytepeec ffu rsxS oan;frBt and Beta for domains; S1 six or four of presence the by characterized is class Oligoflexia The . 64 . 55,56 54 u aaas ofimtesprto fti ls noasprt n o a for one separate a into class this of separation the confirm also data Our . . 53 oee,teAiihoaillscaswspeiul lsie spr of part as classified previously was class Acidithiobacillales the However, . 63 hl lmda n ercmcoi r osdrdevolutionarily considered are Verrucomicrobia and Clamydiae Phyla . 62 hspyu otissxS oan Fgr 4). 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Data may be preliminary. yolsa rgnt ihrfo omnacso ihGa-oiiebcei,o rmdffrn bacte- different from or or bacteria, bacteria Gram-positive Gram-positive with ancestor some common of ria a Tenere- evolution from (phylum the either originate Mollicutes of mycoplasmas branch bacteria regressive parasitic binding a the RNA Firmicutes are from of (Mollicutes) protein functions mycoplasmas basic S1 that the ribosomal performs 30S effectively bacterial cutes) Terrabacteria. the supergroup the that in Note predominantly phyla also other it than data, ancient our more to Chlo- is Cyanobacteria, according domains Actinobacteria, Firmicutes S1 phyla phylum four the the has to and close another Deinococcus-Thermus, Evolutionary to and According close roflexi, domains. evolutionarily Chloroflexi. S1 more phylum four are the have Chloroflexi in predominantly phy- and domains Chloroflexi Actinobacteria S1 phyla the four the in and version, Cyanobacteria arose Eon of Archean phylum photosynthesis number the the anoxygenic a during in of However, photosynthesis domains oxygenic forms occurs. of earliest invention metabolism the the this of before which lum assumptions one in on that taxa, based argued bacterial is have existing understanding studies few the on of based much hypotheses and phototrophy, and anoxygenic of Cyanobacterial history of evolutionary as and lineages well ancient as phyla in phyla, devoloped Deinococcus-Thermus Firmicutes photosynthesis and and Tenerecutes, Chloroflexi, 4). Actinobacteria, Cyanobacteria, (Figure the the containing six supergroup to a one are from Terrabacteria vary can domains areas S1 unexploited structural and of soils, greenhouse fields, cultivated including hsrsac a uddb h usa cec onain rn ubr18-14-00321. number grant more Foundation, the Science while Russian the off”, by “cut funded are was domains research S1 This terminal the that bacterial likely the more Acknowledgements for is sin- that preserved. to it suggest assemblies are time, multirepeat will ones same obtained from central phyla the evolved amino conservative the bacterial At proteins the on the of of Based repeat. development for specificity evolutionary gle relationships the substitutions. the evolutionary as synonymous proteins, the accessed well the S1 and domains, as ribosomal of non-synonymous be S1 domain, study of RNA-binding individual can the ratio structural each data, the in which of formed site and number independently/dependently server, binding the composition be RNA in acid the can conserved change mo- S1 phyla a the into such of bacterial logo with how presence integrated accordance multidomain and demonstrate in were we ribosome evolution composition phyla, important data during different acid functionally 24 structured in amino and and identified largest identity, collected the percentage in The at the ratio analyzed dN/dS protein. and the and collected tifs, have we Here in domains S1 structural the of number respect Conclusions phylogenetic the the ranking bacteria in and in earlier decreasing have domains the of divisions S1 Moreover, likelihood ancient it. structural the phylogenetic six). of greater more (basically secondly, number the domains and structural microorganism, the life firstly, of symbiotic has number that, Tenerecutes during greater argued phylum coincide a be may the phyla can from different it protein of above, S1 the ribosomal con- all 30S G+C Summarizing low the a data, with our bacteria domain. to Gram-positive S1 are According one (Firmicutes) DNA. clostridia clostridia their to of closest in ancestors phylogenetically tent likely are most mycoplasmas the that rea- showed turn, Firmicutes a sequences phylum In RNA the Streptococcus, 16S with and of relationship Lactobacillus, evolutionary analysis their detailed Bacillus, about Clostridium, made genera was assumption the sonable from bacteria Gram-positive and http://oka.protres.ru:4200 72 ae nacmaio fte1SrN lgncetd eune fsvrlseiso mycoplasmas of species several of sequences oligonucleotide rRNA 16S the of comparison a on Based . 72 hshptei a ofimdeprmnal n scniee ntopsil ains all variants: possible two in considered is and experimentally confirmed was hypothesis This . 70,71 enhl,acrigto according meanwhile, . nti oprtv nlsso 33S rti eune hthv been have that sequences protein S1 1333 of analysis comparative this In . 32,70 10 h hlmDioocsTems(v 1domains) S1 (five Deinococcus-Thermus phylum the 67 40 u eyltl skonaottenature the about known is little very but , hr sa supini h literature the in assumption an is There . 29,52 66 oeta o hs hl,tenumber the phyla, these for that Note . ti ieyacpe htoxygenic that accepted widely is It . 68,69 32 u aarvae he S1 three revealed data Our . oe htActinobacteria that Note, . 73,74 more A . 75 . Posted on Authorea 19 Nov 2020 — The copyright holder is the author/funder. All rights reserved. No reuse without permission. — https://doi.org/10.22541/au.160577285.57603701/v1 — This a preprint and has not been peer reviewed. Data may be preliminary. 5 urirTkd ,SbaainA,Cl E h ciiyo iceefamnso ri- manner. substrate-dependant of a in fragments modules C-terminal four discrete ribosomal S1 S1 function. the the by of endoribonuclease between RegB replicase Chem cooperation the activity of Biol to Activation F. due beta Bontems The is M, Uzan protein S, Q PE. Laalami ri- M, Bisaglia coli 16. Cole in Escherichia AR, the S1 of Subramanian http://www.ncbi.nlm.nih.gov/pubmed/6358207 protein repeat C, RNA-binding bosomal last control. Guerrier-Takada autogenous The 15. in M. involved Dreyfus specifically VS, is doi:10.1128/JB.182.20.5872-5879.2000 Artamonova S1 V, protein bosomal I S1. Boni protein 14. ribosomal http://www.ncbi.nlm.nih.gov/pubmed/6348874 of 2012. 2, functions November and Accessed Structure 1983;28:101-142. AR. Escherichia Subramanian of synthesis. 13. S1 own protein its Ribosomal http://www.ncbi.nlm.nih.gov/pubmed/2120211 of S. regulation 2017. Pedersen the 19, AR, for January Subramanian effector MD, the Rasmussen is J, coli ribosomal Schnier of J, fold Skouv OB 12. second the tmRNA. of of all, Contribution recognition M. not doi:10.1271/bbb.68.2319 the Kimura to if 2325. CW, coli most, Escherichia Zwieb of from J, S1 translation Wower protein IK, for Wower required T, is Okada vivo. S1 11. in protein coli ribo- Ribosomal Escherichia the S. in Pedersen in mRNAs J, natural domains Fricke bacteria. of MA, of Sørensen number grouping 10. The phylogenetic the V. of O Galzitskaya hallmark a OM, doi:10.1371/journal.pone.0221370 Selivanova as family. EI, S1 OB-fold Deryusheva protein somal V, the A of and Machulin members repeats, 9. distribution, as Taxonomic proteins V. domain-containing O Galzitskaya S1 Bioinforma OM, structure. the Selivanova tertiary V., of the bet- A functions of relationship Machulin studies the EI, from Deryusheva of derived 8. Investigation functions V. molecular O its Galzitskaya doi:10.3390/molecules24203681 and MA, 2019;24(20):3681. domain Matyunin tendency S1 V., and the A flexibility ween Machulin proteins: EI, S1 Deryusheva in 7. Repeats O. Galzitskaya M, disorder. To- Lobanov intrinsic E, proteins: for Deryusheva Ribosomal A, C. Machulin Brochier-Armanet systematics? 6. V, prokaryotic Daubin for R, standard Planel generation doi:10.1016/j.ympev.2014.02.013 E, next Talla a M, ward Groussin com- HG, in Ramulu proteins 5. ribosomal scale. of domain analysis the Comparative at O. evolution doi:10.1093/nar/gkf693 Poch reductive 5390. D, of Moras example J-C, an Thierry genomes: R, plete Ripp O, Lecompte evolution. A 4. ribosomal S of signatures U Molecular Z. Sci Luthey-Schulten Acad CR, assembly Woese Natl J, ribosomal Proc Montoya A, in Sethi r-proteins E, Roberts of 3. evolution the elucidates conservation O, Residue function. Lespinet RP. and proteins. Bahadur SP, ribosomal prokaryotic Pilla of 2. Phylogenomics YI. Wolf V, E ed. Koonin Puigb`o P, N, Yutin 1. 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Volume Vol . 14 067MY:4.doi:10.3389/fmicb.2016.00744 2016;7(MAY):744. . ESMcoilRev Microbiol FEMS htsnhRes Photosynth lnclImnlg:Picpe and Principles Immunology: Clinical o Evol Mol J M vlBiol Evol BMC 2013;37(5):634-663. . 2007;64(1):90-100. . 1992;33(2):91-111. . cec 8-) (80- Science ESMicrobiol FEMS 2008;8(1):272. . eoeBiol Genome . Posted on Authorea 19 Nov 2020 — The copyright holder is the author/funder. All rights reserved. No reuse without permission. — https://doi.org/10.22541/au.160577285.57603701/v1 — This a preprint and has not been peer reviewed. Data may be preliminary. +Friue ail ,2 15 6 4 4 2, Caldisericia 1, Aquificae 1 Caldiserica 4 Aquificae Bacilli Mollicutes Caldilineae Tenericutes Firmicutes Chloroflexi 3 Deinococcus- Gloeobacteria Cyanobacteria 6 18 Acidobacteriia Acidobacteria 4 3, 2, 1, G+ Actinobacteria Actinobacteria G- Terrabacteria 9 G- 8 G- 7 6 G+ 5 G- 4 3 2 1 1. Table termini the to are due domains. profiles shift the Logo account 4. site. into binding binding Figure taking RNA RNA given the the are domains. to to positions structural correspond The correspond the R70 server. domain of 3 and second WebLogo N68 the the H34, by in L20, generated H29 F17, and residues F17 conserved and The domain first the site. in R66 F17, F14, from 3 protein Figure S1 ( containing Deinococcus-Thermus. five-domain phylum the within for sequence proteins S1 containing five-domain 2. Figure ( 2020 of progress in projects domains, 1. Figure codon. tryptophan UGA legends a Figure of use genes; urease doi:10.1111/j.1365-2958.1990.tb00636.x urealyticum 1990;4(4):669-676. Ureaplasma A. MS. Vonsky Blanchard VM, 75. Chernov OA, Chernova SN, corre- Borkhsenius pulmonis Mycoplasma 74. of chromosome the switching. in phenotypic rearrangements with High-frequency late K. Dybvig B, Bhugra 73. microbial prokaryotes. of other and potential mycoplasmas coding doi:10.1099/00207713-42-2-226 between and 1979;1:43-61. relationships phylogeny Phylogenetic the H. into Neimark Insights 72. genes: al. conserved et using A, genomes Sczyrba matter. P, archaeal dark Schwientek and C, bacterial Rinke of 71. Phylogeny ed. JA. PJ, Planet Eisen supermatrices. AE, and supertrees Darling JM, Lang 70. (c,d) b etrso hlgntcdsrbto frbsmlS proteins S1 ribosomal of distribution phylogenetic of Features . mgso h oomtffrtetidadfut oan fS rtiscnann i domains. six containing proteins S1 of domains fourth and third the for motif Logo the of Images ( 1poenpyu-ee eune distribution, sequences phylum-level protein S1 a b) (a, i hrssoigtedsrbto fbceilS proteins, S1 bacterial of distribution the showing charts Pie ceai ersnaieo h atra hl,cnann ieetnme fsrcua S1 structural of number different containing phyla, bacterial the of representative Schematic a) Nature I nlsso ordmi otiigS rtisfrbceilpya ( phyla. bacterial for proteins S1 containing four-domain of analysis PID ehdSprrusPyu Class Phylum Supergroups method staining Gram oomtfrpeetto o 1poen,cnann w oan.Tecnevdresidues conserved The domains. two containing proteins, S1 for representation motif Logo 034975)4147 doi:10.1038/nature12352 2013;499(7459):431-437. . https://gold.jgi.doe.gov/statistics o Microbiol Mol LSOne PLoS 9269:1915.doi:10.1111/j.1365-2958.1992.tb01553.x 1992;6(9):1149-1154. . 15 Thermus 0384:650 doi:10.1371/journal.pone.0062510 2013;8(4):e62510. . hru thermophilus Thermus c hlgntcdsrbto fbceilgenome bacterial of distribution phylogenetic ) yolsa i Russian] [in Mycoplasmas lsrda2 4 2, 3 Clostridia - 4 Coriobacteriia encci5 Deinococci a ntenme fsrcua S1 structural of number the in c) nPo Dadaioacid amino and ID UniProt . b) h mycoplasmas The domains S1 of Number ak;2002. Nauka; . I nlssfor analysis PID o Microbiol Mol aae,% dataset, from number sequence of Ratio < < < < < < < < < < . . 1 1 1 1 1 1 1 1 1 1 Posted on Authorea 19 Nov 2020 — The copyright holder is the author/funder. All rights reserved. No reuse without permission. — https://doi.org/10.22541/au.160577285.57603701/v1 — This a preprint and has not been peer reviewed. Data may be preliminary. 4SnrittsSnrita5 6 Synergistia Spirochaetia Synergistetes Spirochaetes 6 5, Phycisphaerae 6 5, Chlamydiia 6 Methylacidiphilae5, Chlamydiae Verrucomicrobia G- 1333 Alpha records: Proteobacteria of amount Proteobacteria Total 24 23 G- G- 22 21 20 19 . .0 .8 .7 .3 8.526 6.742 4.124 6.686 7.989 10.88 8.131 10.14 9.237 5.992 3.233 6.063 8.465 10.46 7.811 10.10 7.775 7.390 3.097 5.610 8.171 11.90 6.665 11.16 7.681 7.865 3.306 6.005 9.427 8.232 4.799 10.66 7.407 6.467 3.758 6.135 9.618 11.82 7.517 10.17 6.0 6.3 6.6 7.3 8.7 9.1 9.4 S1domains structural of 9.6 Number S1domains structural of G Number A S1domains structural of N Number I S1domains structural of Number L S1domains V structural of Number K S1domains E structural of Number code letter acid Amino 6 domains. structural 2. Table Nitrospira 6 3 Nitrospirae Fusobacteriia Nitrospinae/TectomicrobiaNitrospinia 6 6 Fusobacteria Deferribacteres Deferribacteres 6 6 Bacteroidia 6 6 Ignavibacteria Bacteroidetes Ignavibacteriae Fibrobacteria GemmatimonadetesGemmatimonadetes6 Chlorobia Fibrobacteres Chlorobi FCB 18 17 16 G- 15 14 13 12 11 10 otn faioai eius()i eune fS iooa rtisb h ubrof number the by proteins ribosomal S1 of sequences in (%) residues acid amino of Content 1333 records: of amount Total ehdSprrusPyu Class Phylum Supergroups method staining Gram n w he orfiesix five four three two one 1333 records: of amount Total 6 4, Planctomycetia Planctomycetes PVC 16 1333 records: of amount Total lgflxa4 6 4, 2 Oligoflexia 6 Acidithiobacillia Epsilonproteobacteria6 8 30 proteobacteria Delta Gammaproteobacteria1, 6 6 4, Betaproteobacteria2, 5, 3, 2, proteobacteria 1333 records: of amount Total 6 2 - 6 4, 6 1, 6 Sphingobacteriia Flavobacteriia Cytophagia ,62 12 6 5, 6 5, domains S1 of Number 1333 records: of amount Total < < < < < < < < 1333 records: of amount Total aae,% dataset, from number sequence of Ratio < < < < < < < < < < < 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 Posted on Authorea 19 Nov 2020 — The copyright holder is the author/funder. All rights reserved. No reuse without permission. — https://doi.org/10.22541/au.160577285.57603701/v1 — This a preprint and has not been peer reviewed. Data may be preliminary. . .8 .1 .2 .9 0.301 1.124 1.585 1.330 1.524 3.020 2.380 5.031 4.346 5.680 7.247 3.192 0.297 1.010 1.462 1.414 1.486 3.863 4.553 5.873 4.422 5.397 5.992 2.865 0.020 0.907 1.834 1.532 0.987 3.659 3.054 5.285 4.274 6.138 7.518 3.009 0.218 0.367 1.756 1.492 2.353 3.995 2. Figure 4.282 6.590 4.788 6.188 6.211 3.766 0.386 0.773 1.271 1.990 1.824 2.653 3.316 4.367 1. Figure 4.864 6.412 6.135 3.095 0.5 0.7 1.9 2.0 2.3 3.0 3.5 3.6 3.9 C 4.5 S1domains structural W of 5.1 Number H 5.9 S1domains structural of Y Number M S1domains structural of Q Number P S1domains structural of Number R S1domains T structural of Number S S1domains D structural of Number F code letter acid Amino 17 Posted on Authorea 19 Nov 2020 — The copyright holder is the author/funder. All rights reserved. No reuse without permission. — https://doi.org/10.22541/au.160577285.57603701/v1 — This a preprint and has not been peer reviewed. Data may be preliminary. iue4. Figure 3. Figure 18