RPAB2_YEAST
ID RPAB2_YEAST Reviewed; 155 AA.
AC P20435; D6W4I7;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC2;
DE Short=RNA polymerases I, II, and III subunit ABC2;
DE AltName: Full=ABC23;
DE AltName: Full=DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide;
GN Name=RPO26; Synonyms=RPB6; OrderedLocusNames=YPR187W; ORFNames=P9677.8;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2186966; DOI=10.1101/gad.4.3.313;
RA Woychik N.A., Liao S.-M., Kolodziej P.A., Young R.A.;
RT "Subunits shared by eukaryotic nuclear RNA polymerases.";
RL Genes Dev. 4:313-323(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2247052; DOI=10.1128/mcb.10.12.6123-6131.1990;
RA Archambault J., Schappert K.T., Friesen J.D.;
RT "A suppressor of an RNA polymerase II mutation of Saccharomyces cerevisiae
RT encodes a subunit common to RNA polymerases I, II, and III.";
RL Mol. Cell. Biol. 10:6123-6131(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=11717393; DOI=10.1073/pnas.231181398;
RA Fath S., Milkereit P., Peyroche G., Riva M., Carles C., Tschochner H.;
RT "Differential roles of phosphorylation in the formation of transcriptional
RT active RNA polymerase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14334-14339(2001).
RN [6]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=11918799; DOI=10.1046/j.1365-2958.2002.02824.x;
RA Van Mullem V., Landrieux E., Vandenhaute J., Thuriaux P.;
RT "Rpa12p, a conserved RNA polymerase I subunit with two functional
RT domains.";
RL Mol. Microbiol. 43:1105-1113(2002).
RN [7]
RP IDENTIFICATION IN THE RNA POL I COMPLEX, AND INTERACTION WITH RPA43.
RX PubMed=12407181; DOI=10.1073/pnas.232580799;
RA Peyroche G., Levillain E., Siaut M., Callebaut I., Schultz P., Sentenac A.,
RA Riva M., Carles C.;
RT "The A14-A43 heterodimer subunit in yeast RNA pol I and their relationship
RT to Rpb4-Rpb7 pol II subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14670-14675(2002).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP REVIEW ON THE RNA POL III COMPLEX, AND PHOSPHORYLATION.
RX PubMed=10384303; DOI=10.1101/sqb.1998.63.381;
RA Chedin S., Ferri M.L., Peyroche G., Andrau J.-C., Jourdain S., Lefebvre O.,
RA Werner M., Carles C., Sentenac A.;
RT "The yeast RNA polymerase III transcription machinery: a paradigm for
RT eukaryotic gene activation.";
RL Cold Spring Harb. Symp. Quant. Biol. 63:381-389(1998).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP ELECTRON MICROSCOPY OF THE RNA POL II/TFIIF COMPLEX.
RX PubMed=14580350; DOI=10.1016/s1097-2765(03)00387-3;
RA Chung W.H., Craighead J.L., Chang W.H., Ezeokonkwo C., Bareket-Samish A.,
RA Kornberg R.D., Asturias F.J.;
RT "RNA polymerase II/TFIIF structure and conserved organization of the
RT initiation complex.";
RL Mol. Cell 12:1003-1013(2003).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
RX PubMed=11313498; DOI=10.1126/science.1059493;
RA Cramer P., Bushnell D.A., Kornberg R.D.;
RT "Structural basis of transcription: RNA polymerase II at 2.8 A
RT resolution.";
RL Science 292:1863-1876(2001).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
RX PubMed=11313499; DOI=10.1126/science.1059495;
RA Gnatt A.L., Cramer P., Fu J., Bushnell D.A., Kornberg R.D.;
RT "Structural basis of transcription: an RNA polymerase II elongation complex
RT at 3.3 A resolution.";
RL Science 292:1876-1882(2001).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX IN
RP COMPLEX WITH ALPHA-AMANITIN.
RX PubMed=11805306; DOI=10.1073/pnas.251664698;
RA Bushnell D.A., Cramer P., Kornberg R.D.;
RT "Structural basis of transcription: alpha-amanitin-RNA polymerase II
RT cocrystal at 2.8 A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1218-1222(2002).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN COMPLEX
RP WITH DST1.
RX PubMed=12914699; DOI=10.1016/s0092-8674(03)00598-1;
RA Kettenberger H., Armache K.J., Cramer P.;
RT "Architecture of the RNA polymerase II-TFIIS complex and implications for
RT mRNA cleavage.";
RL Cell 114:347-357(2003).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS) OF THE RNA POL II COMPLEX.
RX PubMed=12746495; DOI=10.1073/pnas.1030608100;
RA Armache K.J., Kettenberger H., Cramer P.;
RT "Architecture of initiation-competent 12-subunit RNA polymerase II.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:6964-6968(2003).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
RX PubMed=12746498; DOI=10.1073/pnas.1130601100;
RA Bushnell D.A., Kornberg R.D.;
RT "Complete, 12-subunit RNA polymerase II at 4.1-A resolution: implications
RT for the initiation of transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:6969-6973(2003).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
RX PubMed=15537538; DOI=10.1016/j.cell.2004.10.016;
RA Westover K.D., Bushnell D.A., Kornberg R.D.;
RT "Structural basis of transcription: nucleotide selection by rotation in the
RT RNA polymerase II active center.";
RL Cell 119:481-489(2004).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS).
RX PubMed=15610738; DOI=10.1016/j.molcel.2004.11.040;
RA Kettenberger H., Armache K.J., Cramer P.;
RT "Complete RNA polymerase II elongation complex structure and its
RT interactions with NTP and TFIIS.";
RL Mol. Cell 16:955-965(2004).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS) OF THE RNA POL II CORE COMPLEX.
RX PubMed=14963322; DOI=10.1126/science.1090838;
RA Bushnell D.A., Westover K.D., Davis R.E., Kornberg R.D.;
RT "Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at
RT 4.5 Angstroms.";
RL Science 303:983-988(2004).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX.
RX PubMed=15591044; DOI=10.1074/jbc.m413038200;
RA Armache K.J., Mitterweger S., Meinhart A., Cramer P.;
RT "Structures of complete RNA polymerase II and its subcomplex, Rpb4/7.";
RL J. Biol. Chem. 280:7131-7134(2005).
RN [23]
RP 3D-STRUCTURE MODELING OF THE POL III CORE COMPLEX.
RX PubMed=16818233; DOI=10.1016/j.molcel.2006.05.013;
RA Jasiak A.J., Armache K.J., Martens B., Jansen R.P., Cramer P.;
RT "Structural biology of RNA polymerase III: subcomplex C17/25 X-ray
RT structure and 11 subunit enzyme model.";
RL Mol. Cell 23:71-81(2006).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN COMPLEX
RP WITH INHIBITING NON-CODING RNA.
RX PubMed=16341226; DOI=10.1038/nsmb1032;
RA Kettenberger H., Eisenfuhr A., Brueckner F., Theis M., Famulok M.,
RA Cramer P.;
RT "Structure of an RNA polymerase II-RNA inhibitor complex elucidates
RT transcription regulation by noncoding RNAs.";
RL Nat. Struct. Mol. Biol. 13:44-48(2006).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (4.15 ANGSTROMS) OF THE RNA POL II COMPLEX.
RX PubMed=16765890; DOI=10.1016/j.str.2006.04.003;
RA Meyer P.A., Ye P., Zhang M., Suh M.H., Fu J.;
RT "Phasing RNA polymerase II using intrinsically bound Zn atoms: an updated
RT structural model.";
RL Structure 14:973-982(2006).
RN [26]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF THE POL I COMPLEX,
RP FUNCTION, AND SUBUNIT.
RX PubMed=18160037; DOI=10.1016/j.cell.2007.10.051;
RA Kuhn C.D., Geiger S.R., Baumli S., Gartmann M., Gerber J., Jennebach S.,
RA Mielke T., Tschochner H., Beckmann R., Cramer P.;
RT "Functional architecture of RNA polymerase I.";
RL Cell 131:1260-1272(2007).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153184; DOI=10.1038/nature12636;
RA Fernandez-Tornero C., Moreno-Morcillo M., Rashid U.J., Taylor N.M.,
RA Ruiz F.M., Gruene T., Legrand P., Steuerwald U., Muller C.W.;
RT "Crystal structure of the 14-subunit RNA polymerase I.";
RL Nature 502:644-649(2013).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153182; DOI=10.1038/nature12712;
RA Engel C., Sainsbury S., Cheung A.C., Kostrewa D., Cramer P.;
RT "RNA polymerase I structure and transcription regulation.";
RL Nature 502:650-655(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Common component of RNA polymerases I, II and III which synthesize
CC ribosomal RNA precursors, mRNA precursors and many functional non-
CC coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
CC Pol II is the central component of the basal RNA polymerase II
CC transcription machinery. RNA polymerases are composed of mobile
CC elements that move relative to each other. In Pol II, RPB6 is part of
CC the clamp element and together with parts of RPB1 and RPB2 forms a
CC pocket to which the RPB4-RPB7 subcomplex binds.
CC {ECO:0000269|PubMed:18160037, ECO:0000269|PubMed:24153182,
CC ECO:0000269|PubMed:24153184}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II
CC (Pol II) and RNA polymerase III (Pol III) complexes. Component of the
CC RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135,
CC RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19,
CC RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped
CC core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10,
CC RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-
CC binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that
CC mediates interactions with transcription initiation factors and newly
CC synthesized RNA. Component of the RNA polymerase II (Pol II) complex
CC consisting of 12 subunits: RPO21, RPB2, RPB3, RPB4, RPB5, RPO26, RPB7,
CC RPB8, RPB9, RPB10 and RPC10. Component of the RNA polymerase III (Pol
CC III) complex consisting of 17 subunits. {ECO:0000269|PubMed:11717393,
CC ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:11918799,
CC ECO:0000269|PubMed:12407181, ECO:0000269|PubMed:12914699,
CC ECO:0000269|PubMed:16341226, ECO:0000269|PubMed:18160037,
CC ECO:0000269|PubMed:24153182, ECO:0000269|PubMed:24153184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 6090 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; X53288; CAA37382.1; -; Genomic_DNA.
DR EMBL; M33924; AAA34989.1; -; Genomic_DNA.
DR EMBL; U25841; AAB64616.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11603.1; -; Genomic_DNA.
DR PIR; S13307; RNBYR6.
DR RefSeq; NP_015513.1; NM_001184284.1.
DR PDB; 1I3Q; X-ray; 3.10 A; F=1-155.
DR PDB; 1I50; X-ray; 2.80 A; F=1-155.
DR PDB; 1I6H; X-ray; 3.30 A; F=1-155.
DR PDB; 1K83; X-ray; 2.80 A; F=1-155.
DR PDB; 1NIK; X-ray; 4.10 A; F=1-155.
DR PDB; 1NT9; X-ray; 4.20 A; F=1-155.
DR PDB; 1PQV; X-ray; 3.80 A; F=1-155.
DR PDB; 1R5U; X-ray; 4.50 A; F=1-155.
DR PDB; 1R9S; X-ray; 4.25 A; F=1-155.
DR PDB; 1R9T; X-ray; 3.50 A; F=1-155.
DR PDB; 1SFO; X-ray; 3.61 A; F=1-155.
DR PDB; 1TWA; X-ray; 3.20 A; F=1-155.
DR PDB; 1TWC; X-ray; 3.00 A; F=1-155.
DR PDB; 1TWF; X-ray; 2.30 A; F=1-155.
DR PDB; 1TWG; X-ray; 3.30 A; F=1-155.
DR PDB; 1TWH; X-ray; 3.40 A; F=1-155.
DR PDB; 1WCM; X-ray; 3.80 A; F=1-155.
DR PDB; 1Y1V; X-ray; 3.80 A; F=1-155.
DR PDB; 1Y1W; X-ray; 4.00 A; F=1-155.
DR PDB; 1Y1Y; X-ray; 4.00 A; F=1-155.
DR PDB; 1Y77; X-ray; 4.50 A; F=1-155.
DR PDB; 2B63; X-ray; 3.80 A; F=1-155.
DR PDB; 2B8K; X-ray; 4.15 A; F=1-155.
DR PDB; 2E2H; X-ray; 3.95 A; F=1-155.
DR PDB; 2E2I; X-ray; 3.41 A; F=1-155.
DR PDB; 2E2J; X-ray; 3.50 A; F=1-155.
DR PDB; 2JA5; X-ray; 3.80 A; F=1-155.
DR PDB; 2JA6; X-ray; 4.00 A; F=1-155.
DR PDB; 2JA7; X-ray; 3.80 A; F/R=1-155.
DR PDB; 2JA8; X-ray; 3.80 A; F=1-155.
DR PDB; 2NVQ; X-ray; 2.90 A; F=1-155.
DR PDB; 2NVT; X-ray; 3.36 A; F=1-155.
DR PDB; 2NVX; X-ray; 3.60 A; F=1-155.
DR PDB; 2NVY; X-ray; 3.40 A; F=1-155.
DR PDB; 2NVZ; X-ray; 4.30 A; F=1-155.
DR PDB; 2R7Z; X-ray; 3.80 A; F=1-155.
DR PDB; 2R92; X-ray; 3.80 A; F=1-155.
DR PDB; 2R93; X-ray; 4.00 A; F=1-155.
DR PDB; 2VUM; X-ray; 3.40 A; F=1-155.
DR PDB; 2YU9; X-ray; 3.40 A; F=1-155.
DR PDB; 3CQZ; X-ray; 2.80 A; F=1-155.
DR PDB; 3FKI; X-ray; 3.88 A; F=1-155.
DR PDB; 3GTG; X-ray; 3.78 A; F=1-155.
DR PDB; 3GTJ; X-ray; 3.42 A; F=1-155.
DR PDB; 3GTK; X-ray; 3.80 A; F=1-155.
DR PDB; 3GTL; X-ray; 3.38 A; F=1-155.
DR PDB; 3GTM; X-ray; 3.80 A; F=1-155.
DR PDB; 3GTO; X-ray; 4.00 A; F=1-155.
DR PDB; 3GTP; X-ray; 3.90 A; F=1-155.
DR PDB; 3GTQ; X-ray; 3.80 A; F=1-155.
DR PDB; 3H3V; X-ray; 4.00 A; G=1-155.
DR PDB; 3HOU; X-ray; 3.20 A; F/R=1-155.
DR PDB; 3HOV; X-ray; 3.50 A; F=1-155.
DR PDB; 3HOW; X-ray; 3.60 A; F=1-155.
DR PDB; 3HOX; X-ray; 3.65 A; F=1-155.
DR PDB; 3HOY; X-ray; 3.40 A; F=1-155.
DR PDB; 3HOZ; X-ray; 3.65 A; F=1-155.
DR PDB; 3I4M; X-ray; 3.70 A; F=1-155.
DR PDB; 3I4N; X-ray; 3.90 A; F=1-155.
DR PDB; 3J0K; EM; 36.00 A; F=72-155.
DR PDB; 3J1N; EM; 16.00 A; F=72-155.
DR PDB; 3K1F; X-ray; 4.30 A; F=1-155.
DR PDB; 3K7A; X-ray; 3.80 A; F=1-155.
DR PDB; 3M3Y; X-ray; 3.18 A; F=1-155.
DR PDB; 3M4O; X-ray; 3.57 A; F=1-155.
DR PDB; 3PO2; X-ray; 3.30 A; F=1-155.
DR PDB; 3PO3; X-ray; 3.30 A; F=1-155.
DR PDB; 3QT1; X-ray; 4.30 A; F=1-155.
DR PDB; 3RZD; X-ray; 3.30 A; F=1-155.
DR PDB; 3RZO; X-ray; 3.00 A; F=1-155.
DR PDB; 3S14; X-ray; 2.85 A; F=1-155.
DR PDB; 3S15; X-ray; 3.30 A; F=1-155.
DR PDB; 3S16; X-ray; 3.24 A; F=1-155.
DR PDB; 3S17; X-ray; 3.20 A; F=1-155.
DR PDB; 3S1M; X-ray; 3.13 A; F=1-155.
DR PDB; 3S1N; X-ray; 3.10 A; F=1-155.
DR PDB; 3S1Q; X-ray; 3.30 A; F=1-155.
DR PDB; 3S1R; X-ray; 3.20 A; F=1-155.
DR PDB; 3S2D; X-ray; 3.20 A; F=1-155.
DR PDB; 3S2H; X-ray; 3.30 A; F=1-155.
DR PDB; 4A3B; X-ray; 3.50 A; F=1-155.
DR PDB; 4A3C; X-ray; 3.50 A; F=1-155.
DR PDB; 4A3D; X-ray; 3.40 A; F=1-155.
DR PDB; 4A3E; X-ray; 3.40 A; F=1-155.
DR PDB; 4A3F; X-ray; 3.50 A; F=1-155.
DR PDB; 4A3G; X-ray; 3.50 A; F=1-155.
DR PDB; 4A3I; X-ray; 3.80 A; F=1-155.
DR PDB; 4A3J; X-ray; 3.70 A; F=1-155.
DR PDB; 4A3K; X-ray; 3.50 A; F=1-155.
DR PDB; 4A3L; X-ray; 3.50 A; F=1-155.
DR PDB; 4A3M; X-ray; 3.90 A; F=1-155.
DR PDB; 4A93; X-ray; 3.40 A; F=1-155.
DR PDB; 4BBR; X-ray; 3.40 A; F=1-155.
DR PDB; 4BBS; X-ray; 3.60 A; F=1-155.
DR PDB; 4BXX; X-ray; 3.28 A; F=1-155.
DR PDB; 4BXZ; X-ray; 4.80 A; F=1-155.
DR PDB; 4BY1; X-ray; 3.60 A; F=1-155.
DR PDB; 4BY7; X-ray; 3.15 A; F=1-155.
DR PDB; 4C2M; X-ray; 2.80 A; F/U=1-155.
DR PDB; 4C3H; X-ray; 3.27 A; F=1-155.
DR PDB; 4C3I; X-ray; 3.00 A; F=1-155.
DR PDB; 4C3J; X-ray; 3.35 A; F=1-155.
DR PDB; 4V1M; EM; 6.60 A; F=1-155.
DR PDB; 4V1N; EM; 7.80 A; F=1-155.
DR PDB; 4V1O; EM; 9.70 A; F=1-155.
DR PDB; 4X67; X-ray; 4.10 A; F=1-155.
DR PDB; 4X6A; X-ray; 3.96 A; F=1-155.
DR PDB; 4Y52; X-ray; 3.50 A; F=1-155.
DR PDB; 4Y7N; X-ray; 3.30 A; F=1-155.
DR PDB; 4YM7; X-ray; 5.50 A; AF/BF/CF/DF/EF/FF=1-155.
DR PDB; 5C3E; X-ray; 3.70 A; F=1-155.
DR PDB; 5C44; X-ray; 3.95 A; F=1-155.
DR PDB; 5C4A; X-ray; 4.20 A; F=1-155.
DR PDB; 5C4J; X-ray; 4.00 A; F=1-155.
DR PDB; 5C4X; X-ray; 4.00 A; F=1-155.
DR PDB; 5FJ8; EM; 3.90 A; F=1-155.
DR PDB; 5FJ9; EM; 4.60 A; F=1-155.
DR PDB; 5FJA; EM; 4.65 A; F=1-155.
DR PDB; 5FMF; EM; 6.00 A; F=72-155.
DR PDB; 5FYW; EM; 4.35 A; F=1-155.
DR PDB; 5FZ5; EM; 8.80 A; F=1-155.
DR PDB; 5G5L; EM; 4.80 A; F=1-155.
DR PDB; 5IP7; X-ray; 3.52 A; F=69-155.
DR PDB; 5IP9; X-ray; 3.90 A; F=69-155.
DR PDB; 5LMX; EM; 4.90 A; F=1-155.
DR PDB; 5M3F; EM; 3.80 A; F=1-155.
DR PDB; 5M3M; EM; 4.00 A; F=1-155.
DR PDB; 5M5W; EM; 3.80 A; F=1-155.
DR PDB; 5M5X; EM; 4.00 A; F=1-155.
DR PDB; 5M5Y; EM; 4.00 A; F=1-155.
DR PDB; 5M64; EM; 4.60 A; F=1-155.
DR PDB; 5N5Y; EM; 7.70 A; F=1-155.
DR PDB; 5N5Z; EM; 7.70 A; F=1-155.
DR PDB; 5N60; EM; 7.70 A; F=1-155.
DR PDB; 5N61; EM; 3.40 A; F=1-155.
DR PDB; 5OA1; EM; 4.40 A; F=1-155.
DR PDB; 5OQJ; EM; 4.70 A; F=1-155.
DR PDB; 5OQM; EM; 5.80 A; F=1-155.
DR PDB; 5OT2; X-ray; 3.20 A; F=1-155.
DR PDB; 5SVA; EM; 15.30 A; F=1-155.
DR PDB; 5U5Q; X-ray; 3.80 A; F=1-155.
DR PDB; 5VVR; EM; 5.80 A; F=1-155.
DR PDB; 5VVS; EM; 6.40 A; F=1-155.
DR PDB; 5W4U; X-ray; 3.60 A; F=1-155.
DR PDB; 5W51; X-ray; 3.40 A; F=1-155.
DR PDB; 5W5Y; EM; 3.80 A; F=1-155.
DR PDB; 5W64; EM; 4.20 A; F=1-155.
DR PDB; 5W65; EM; 4.30 A; F=1-155.
DR PDB; 5W66; EM; 3.90 A; F=1-155.
DR PDB; 6BLO; X-ray; 3.40 A; F=1-155.
DR PDB; 6BLP; X-ray; 3.20 A; F=1-155.
DR PDB; 6BM2; X-ray; 3.40 A; F=1-155.
DR PDB; 6BM4; X-ray; 2.95 A; F=1-155.
DR PDB; 6BQF; X-ray; 3.35 A; F=1-155.
DR PDB; 6CNB; EM; 4.10 A; F=1-155.
DR PDB; 6CNC; EM; 4.10 A; F=1-155.
DR PDB; 6CND; EM; 4.80 A; F=1-155.
DR PDB; 6CNF; EM; 4.50 A; F=1-155.
DR PDB; 6EU0; EM; 4.00 A; F=1-155.
DR PDB; 6EU1; EM; 3.40 A; F=1-155.
DR PDB; 6EU2; EM; 3.40 A; F=1-155.
DR PDB; 6EU3; EM; 3.30 A; F=1-155.
DR PDB; 6F40; EM; 3.70 A; F=1-155.
DR PDB; 6F41; EM; 4.30 A; F=1-155.
DR PDB; 6F42; EM; 5.50 A; F=1-155.
DR PDB; 6F44; EM; 4.20 A; F=1-155.
DR PDB; 6GYK; EM; 5.10 A; F=2-155.
DR PDB; 6GYL; EM; 4.80 A; F=1-155.
DR PDB; 6GYM; EM; 6.70 A; F=1-155.
DR PDB; 6H67; EM; 3.60 A; F=1-155.
DR PDB; 6H68; EM; 4.60 A; F=1-155.
DR PDB; 6HKO; EM; 3.42 A; F=1-155.
DR PDB; 6HLQ; EM; 3.18 A; F=1-155.
DR PDB; 6HLR; EM; 3.18 A; F=1-155.
DR PDB; 6HLS; EM; 3.21 A; F=1-155.
DR PDB; 6I84; EM; 4.40 A; F=1-155.
DR PDB; 6O6C; EM; 3.10 A; E=1-155.
DR PDB; 6RQH; EM; 3.70 A; F=1-155.
DR PDB; 6RQL; EM; 2.90 A; F=1-155.
DR PDB; 6RQT; EM; 4.00 A; F=1-155.
DR PDB; 6RRD; EM; 3.10 A; F=1-155.
DR PDB; 6RUI; EM; 2.70 A; F=1-155.
DR PDB; 6RUO; EM; 3.50 A; F=1-155.
DR PDB; 6RWE; EM; 3.00 A; F=1-155.
DR PDB; 6TPS; EM; 3.54 A; F=1-155.
DR PDB; 6TUT; EM; 3.25 A; F=1-155.
DR PDB; 6UPX; X-ray; 3.40 A; F=1-155.
DR PDB; 6UPY; X-ray; 3.40 A; F=1-155.
DR PDB; 6UPZ; X-ray; 3.10 A; F=1-155.
DR PDB; 6UQ0; X-ray; 3.56 A; F=1-155.
DR PDB; 6UQ1; X-ray; 3.60 A; F=1-155.
DR PDB; 6UQ2; X-ray; 3.20 A; F=1-155.
DR PDB; 6UQ3; X-ray; 3.47 A; F=1-155.
DR PDB; 7KED; X-ray; 3.60 A; F=1-155.
DR PDB; 7KEE; X-ray; 3.45 A; F=1-155.
DR PDB; 7KEF; X-ray; 3.89 A; F=1-155.
DR PDB; 7NKX; EM; 2.90 A; F=1-155.
DR PDB; 7NKY; EM; 3.20 A; F=1-155.
DR PDB; 7O4I; EM; 3.20 A; F=1-155.
DR PDB; 7O4J; EM; 2.90 A; F=1-155.
DR PDB; 7O4K; EM; 3.60 A; F=1-155.
DR PDB; 7O4L; EM; 3.40 A; F=1-155.
DR PDB; 7O72; EM; 3.40 A; F=1-155.
DR PDB; 7O73; EM; 3.40 A; F=1-155.
DR PDB; 7O75; EM; 3.20 A; F=1-155.
DR PDB; 7RIM; X-ray; 2.90 A; F=1-155.
DR PDB; 7RIP; X-ray; 3.30 A; F=1-155.
DR PDB; 7RIQ; X-ray; 3.00 A; F=1-155.
DR PDB; 7RIW; X-ray; 3.20 A; F=1-155.
DR PDB; 7RIX; X-ray; 3.40 A; F=1-155.
DR PDB; 7RIY; X-ray; 3.70 A; F=1-155.
DR PDBsum; 1I3Q; -.
DR PDBsum; 1I50; -.
DR PDBsum; 1I6H; -.
DR PDBsum; 1K83; -.
DR PDBsum; 1NIK; -.
DR PDBsum; 1NT9; -.
DR PDBsum; 1PQV; -.
DR PDBsum; 1R5U; -.
DR PDBsum; 1R9S; -.
DR PDBsum; 1R9T; -.
DR PDBsum; 1SFO; -.
DR PDBsum; 1TWA; -.
DR PDBsum; 1TWC; -.
DR PDBsum; 1TWF; -.
DR PDBsum; 1TWG; -.
DR PDBsum; 1TWH; -.
DR PDBsum; 1WCM; -.
DR PDBsum; 1Y1V; -.
DR PDBsum; 1Y1W; -.
DR PDBsum; 1Y1Y; -.
DR PDBsum; 1Y77; -.
DR PDBsum; 2B63; -.
DR PDBsum; 2B8K; -.
DR PDBsum; 2E2H; -.
DR PDBsum; 2E2I; -.
DR PDBsum; 2E2J; -.
DR PDBsum; 2JA5; -.
DR PDBsum; 2JA6; -.
DR PDBsum; 2JA7; -.
DR PDBsum; 2JA8; -.
DR PDBsum; 2NVQ; -.
DR PDBsum; 2NVT; -.
DR PDBsum; 2NVX; -.
DR PDBsum; 2NVY; -.
DR PDBsum; 2NVZ; -.
DR PDBsum; 2R7Z; -.
DR PDBsum; 2R92; -.
DR PDBsum; 2R93; -.
DR PDBsum; 2VUM; -.
DR PDBsum; 2YU9; -.
DR PDBsum; 3CQZ; -.
DR PDBsum; 3FKI; -.
DR PDBsum; 3GTG; -.
DR PDBsum; 3GTJ; -.
DR PDBsum; 3GTK; -.
DR PDBsum; 3GTL; -.
DR PDBsum; 3GTM; -.
DR PDBsum; 3GTO; -.
DR PDBsum; 3GTP; -.
DR PDBsum; 3GTQ; -.
DR PDBsum; 3H3V; -.
DR PDBsum; 3HOU; -.
DR PDBsum; 3HOV; -.
DR PDBsum; 3HOW; -.
DR PDBsum; 3HOX; -.
DR PDBsum; 3HOY; -.
DR PDBsum; 3HOZ; -.
DR PDBsum; 3I4M; -.
DR PDBsum; 3I4N; -.
DR PDBsum; 3J0K; -.
DR PDBsum; 3J1N; -.
DR PDBsum; 3K1F; -.
DR PDBsum; 3K7A; -.
DR PDBsum; 3M3Y; -.
DR PDBsum; 3M4O; -.
DR PDBsum; 3PO2; -.
DR PDBsum; 3PO3; -.
DR PDBsum; 3QT1; -.
DR PDBsum; 3RZD; -.
DR PDBsum; 3RZO; -.
DR PDBsum; 3S14; -.
DR PDBsum; 3S15; -.
DR PDBsum; 3S16; -.
DR PDBsum; 3S17; -.
DR PDBsum; 3S1M; -.
DR PDBsum; 3S1N; -.
DR PDBsum; 3S1Q; -.
DR PDBsum; 3S1R; -.
DR PDBsum; 3S2D; -.
DR PDBsum; 3S2H; -.
DR PDBsum; 4A3B; -.
DR PDBsum; 4A3C; -.
DR PDBsum; 4A3D; -.
DR PDBsum; 4A3E; -.
DR PDBsum; 4A3F; -.
DR PDBsum; 4A3G; -.
DR PDBsum; 4A3I; -.
DR PDBsum; 4A3J; -.
DR PDBsum; 4A3K; -.
DR PDBsum; 4A3L; -.
DR PDBsum; 4A3M; -.
DR PDBsum; 4A93; -.
DR PDBsum; 4BBR; -.
DR PDBsum; 4BBS; -.
DR PDBsum; 4BXX; -.
DR PDBsum; 4BXZ; -.
DR PDBsum; 4BY1; -.
DR PDBsum; 4BY7; -.
DR PDBsum; 4C2M; -.
DR PDBsum; 4C3H; -.
DR PDBsum; 4C3I; -.
DR PDBsum; 4C3J; -.
DR PDBsum; 4V1M; -.
DR PDBsum; 4V1N; -.
DR PDBsum; 4V1O; -.
DR PDBsum; 4X67; -.
DR PDBsum; 4X6A; -.
DR PDBsum; 4Y52; -.
DR PDBsum; 4Y7N; -.
DR PDBsum; 4YM7; -.
DR PDBsum; 5C3E; -.
DR PDBsum; 5C44; -.
DR PDBsum; 5C4A; -.
DR PDBsum; 5C4J; -.
DR PDBsum; 5C4X; -.
DR PDBsum; 5FJ8; -.
DR PDBsum; 5FJ9; -.
DR PDBsum; 5FJA; -.
DR PDBsum; 5FMF; -.
DR PDBsum; 5FYW; -.
DR PDBsum; 5FZ5; -.
DR PDBsum; 5G5L; -.
DR PDBsum; 5IP7; -.
DR PDBsum; 5IP9; -.
DR PDBsum; 5LMX; -.
DR PDBsum; 5M3F; -.
DR PDBsum; 5M3M; -.
DR PDBsum; 5M5W; -.
DR PDBsum; 5M5X; -.
DR PDBsum; 5M5Y; -.
DR PDBsum; 5M64; -.
DR PDBsum; 5N5Y; -.
DR PDBsum; 5N5Z; -.
DR PDBsum; 5N60; -.
DR PDBsum; 5N61; -.
DR PDBsum; 5OA1; -.
DR PDBsum; 5OQJ; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5OT2; -.
DR PDBsum; 5SVA; -.
DR PDBsum; 5U5Q; -.
DR PDBsum; 5VVR; -.
DR PDBsum; 5VVS; -.
DR PDBsum; 5W4U; -.
DR PDBsum; 5W51; -.
DR PDBsum; 5W5Y; -.
DR PDBsum; 5W64; -.
DR PDBsum; 5W65; -.
DR PDBsum; 5W66; -.
DR PDBsum; 6BLO; -.
DR PDBsum; 6BLP; -.
DR PDBsum; 6BM2; -.
DR PDBsum; 6BM4; -.
DR PDBsum; 6BQF; -.
DR PDBsum; 6CNB; -.
DR PDBsum; 6CNC; -.
DR PDBsum; 6CND; -.
DR PDBsum; 6CNF; -.
DR PDBsum; 6EU0; -.
DR PDBsum; 6EU1; -.
DR PDBsum; 6EU2; -.
DR PDBsum; 6EU3; -.
DR PDBsum; 6F40; -.
DR PDBsum; 6F41; -.
DR PDBsum; 6F42; -.
DR PDBsum; 6F44; -.
DR PDBsum; 6GYK; -.
DR PDBsum; 6GYL; -.
DR PDBsum; 6GYM; -.
DR PDBsum; 6H67; -.
DR PDBsum; 6H68; -.
DR PDBsum; 6HKO; -.
DR PDBsum; 6HLQ; -.
DR PDBsum; 6HLR; -.
DR PDBsum; 6HLS; -.
DR PDBsum; 6I84; -.
DR PDBsum; 6O6C; -.
DR PDBsum; 6RQH; -.
DR PDBsum; 6RQL; -.
DR PDBsum; 6RQT; -.
DR PDBsum; 6RRD; -.
DR PDBsum; 6RUI; -.
DR PDBsum; 6RUO; -.
DR PDBsum; 6RWE; -.
DR PDBsum; 6TPS; -.
DR PDBsum; 6TUT; -.
DR PDBsum; 6UPX; -.
DR PDBsum; 6UPY; -.
DR PDBsum; 6UPZ; -.
DR PDBsum; 6UQ0; -.
DR PDBsum; 6UQ1; -.
DR PDBsum; 6UQ2; -.
DR PDBsum; 6UQ3; -.
DR PDBsum; 7KED; -.
DR PDBsum; 7KEE; -.
DR PDBsum; 7KEF; -.
DR PDBsum; 7NKX; -.
DR PDBsum; 7NKY; -.
DR PDBsum; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 7O4K; -.
DR PDBsum; 7O4L; -.
DR PDBsum; 7O72; -.
DR PDBsum; 7O73; -.
DR PDBsum; 7O75; -.
DR PDBsum; 7RIM; -.
DR PDBsum; 7RIP; -.
DR PDBsum; 7RIQ; -.
DR PDBsum; 7RIW; -.
DR PDBsum; 7RIX; -.
DR PDBsum; 7RIY; -.
DR AlphaFoldDB; P20435; -.
DR SMR; P20435; -.
DR BioGRID; 36359; 109.
DR ComplexPortal; CPX-1664; DNA-directed RNA Polymerase I complex.
DR ComplexPortal; CPX-2660; DNA-directed RNA polymerase III complex.
DR ComplexPortal; CPX-2662; DNA-directed RNA polymerase II complex.
DR DIP; DIP-2194N; -.
DR IntAct; P20435; 43.
DR MINT; P20435; -.
DR STRING; 4932.YPR187W; -.
DR iPTMnet; P20435; -.
DR MaxQB; P20435; -.
DR PaxDb; P20435; -.
DR PRIDE; P20435; -.
DR EnsemblFungi; YPR187W_mRNA; YPR187W; YPR187W.
DR GeneID; 856317; -.
DR KEGG; sce:YPR187W; -.
DR SGD; S000006391; RPO26.
DR VEuPathDB; FungiDB:YPR187W; -.
DR eggNOG; KOG3405; Eukaryota.
DR GeneTree; ENSGT00390000010415; -.
DR HOGENOM; CLU_112527_0_2_1; -.
DR InParanoid; P20435; -.
DR OMA; YNEAPEN; -.
DR BioCyc; YEAST:G3O-34310-MON; -.
DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SCE-72086; mRNA Capping.
DR Reactome; R-SCE-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SCE-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-SCE-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR EvolutionaryTrace; P20435; -.
DR PRO; PR:P20435; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P20435; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:UniProtKB.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:SGD.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0001054; F:RNA polymerase I activity; IDA:UniProtKB.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:ComplexPortal.
DR GO; GO:0006386; P:termination of RNA polymerase III transcription; IDA:ComplexPortal.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IDA:ComplexPortal.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:ComplexPortal.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IDA:ComplexPortal.
DR GO; GO:0001172; P:transcription, RNA-templated; IEA:GOC.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IDA:SGD.
DR DisProt; DP00771; -.
DR Gene3D; 3.90.940.10; -; 1.
DR HAMAP; MF_00192; RNApol_arch_Rpo6; 1.
DR InterPro; IPR020708; DNA-dir_RNA_polK_14-18kDa_CS.
DR InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR InterPro; IPR028363; RPB6.
DR InterPro; IPR036161; RPB6/omega-like_sf.
DR InterPro; IPR006111; Rpo6/Rpb6.
DR Pfam; PF01192; RNA_pol_Rpb6; 1.
DR PIRSF; PIRSF500154; RPB6; 1.
DR PIRSF; PIRSF000778; RpoK/RPB6; 1.
DR SMART; SM01409; RNA_pol_Rpb6; 1.
DR SUPFAM; SSF63562; SSF63562; 1.
DR PROSITE; PS01111; RNA_POL_K_14KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; Transcription.
FT CHAIN 1..155
FT /note="DNA-directed RNA polymerases I, II, and III subunit
FT RPABC2"
FT /id="PRO_0000133797"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..132
FT /note="Leucine-zipper"
FT COMPBIAS 1..24
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 57..71
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:6RQL"
FT HELIX 87..102
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1I3Q"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:6RQL"
SQ SEQUENCE 155 AA; 17910 MW; AA3DEF529F94A5E4 CRC64;
MSDYEEAFND GNENFEDFDV EHFSDEETYE EKPQFKDGET TDANGKTIVT GGNGPEDFQQ
HEQIRRKTLK EKAIPKDQRA TTPYMTKYER ARILGTRALQ ISMNAPVFVD LEGETDPLRI
AMKELAEKKI PLVIRRYLPD GSFEDWSVEE LIVDL
