ID RPAB3_YEAST Reviewed; 146 AA. AC P20436; D6W2S9; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 04-NOV-2026, entry version 232. DE RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC3; DE Short=RNA polymerases I, II, and III subunit ABC3; DE AltName: Full=ABC14.4; DE AltName: Full=ABC14.5; DE AltName: Full=DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide; GN Name=RPB8; OrderedLocusNames=YOR224C; ORFNames=YOR50-14; 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]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=8840505; RX DOI=10.1002/(sici)1097-0061(199607)12:9<877::aid-yea969>3.0.co;2-s; RA Galisson F., Dujon B.; RT "Sequence and analysis of a 33 kb fragment from the right arm of chromosome RT XV of the yeast Saccharomyces cerevisiae."; RL Yeast 12:877-885(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169874; DOI=10.1038/387s098; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [6] RP REVIEW ON THE RNA POL III COMPLEX. 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 [7] RP IDENTIFICATION IN THE RNA POL I COMPLEX. 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-68, 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [12] RP STRUCTURE BY NMR. RX PubMed=9461075; DOI=10.1038/nsb0298-110; RA Krapp S., Kelly G., Reischi J., Weinzierl R.O.J., Matthews S.; RT "Eukaryotic RNA polymerase subunit RPB8 is a new relative of the OB RT family."; RL Nat. Struct. Biol. 5:110-114(1998). RN [13] 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 [14] RP X-RAY CRYSTALLOGRAPHY 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 [15] RP X-RAY CRYSTALLOGRAPHY 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 [16] RP X-RAY CRYSTALLOGRAPHY OF THE RNA POL II CORE COMPLEX IN COMPLEX WITH RP 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 [17] RP X-RAY CRYSTALLOGRAPHY OF THE RNA POL II COMPLEX IN COMPLEX 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 [18] RP X-RAY CRYSTALLOGRAPHY 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 [19] RP X-RAY CRYSTALLOGRAPHY 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 [20] RP X-RAY CRYSTALLOGRAPHY 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 [21] RP X-RAY CRYSTALLOGRAPHY. 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 [22] RP X-RAY CRYSTALLOGRAPHY 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 [23] RP X-RAY CRYSTALLOGRAPHY 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 [24] 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 [25] RP X-RAY CRYSTALLOGRAPHY OF THE RNA POL II COMPLEX IN COMPLEX WITH INHIBITING RP 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 [26] RP X-RAY CRYSTALLOGRAPHY 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 [27] RP STRUCTURE BY ELECTRON MICROSCOPY OF THE POL I COMPLEX, FUNCTION, AND RP 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 [28] RP X-RAY CRYSTALLOGRAPHY OF THE POL I COMPLEX, FUNCTION, AND 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 [29] RP X-RAY CRYSTALLOGRAPHY OF THE POL I COMPLEX, FUNCTION, AND 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 {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. Directly interacts with POLR2A. CC {ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:12407181, CC ECO:0000269|PubMed:12914699, ECO:0000269|PubMed:16341226, CC ECO:0000269|PubMed:18160037, ECO:0000269|PubMed:24153182, CC ECO:0000269|PubMed:24153184}. CC -!- INTERACTION: CC P20436; P38902: RPB11; NbExp=4; IntAct=EBI-15794, EBI-15806; CC P20436; P20434: RPB5; NbExp=35; IntAct=EBI-15794, EBI-15781; CC P20436; P27999: RPB9; NbExp=4; IntAct=EBI-15794, EBI-15798; CC P20436; P47076: RPC17; NbExp=3; IntAct=EBI-15794, EBI-25782; CC P20436; P32910: RPC34; NbExp=3; IntAct=EBI-15794, EBI-15835; CC P20436; P07703: RPC40; NbExp=4; IntAct=EBI-15794, EBI-15831; CC P20436; P39940: RSP5; NbExp=3; IntAct=EBI-15794, EBI-16219; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 6210 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the eukaryotic RPB8 RNA polymerase subunit CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X53289; CAA37383.1; -; Genomic_DNA. DR EMBL; X92441; CAA63187.1; -; Genomic_DNA. DR EMBL; Z75132; CAA99443.1; -; Genomic_DNA. DR EMBL; AY693087; AAT93106.1; -; Genomic_DNA. DR EMBL; BK006948; DAA10995.1; -; Genomic_DNA. DR PIR; C34588; C34588. DR RefSeq; NP_014867.1; NM_001183643.1. DR PDB; 1A1D; NMR; -; A=1-146. DR PDB; 1I3Q; X-ray; 3.10 A; H=1-146. DR PDB; 1I50; X-ray; 2.80 A; H=1-146. DR PDB; 1I6H; X-ray; 3.30 A; H=1-146. DR PDB; 1K83; X-ray; 2.80 A; H=1-146. DR PDB; 1NIK; X-ray; 4.10 A; H=1-146. DR PDB; 1NT9; X-ray; 4.20 A; H=1-146. DR PDB; 1PQV; X-ray; 3.80 A; H=1-146. DR PDB; 1R5U; X-ray; 4.50 A; H=1-146. DR PDB; 1R9S; X-ray; 4.25 A; H=1-146. DR PDB; 1R9T; X-ray; 3.50 A; H=1-146. DR PDB; 1SFO; X-ray; 3.61 A; H=1-146. DR PDB; 1TWA; X-ray; 3.20 A; H=1-146. DR PDB; 1TWC; X-ray; 3.00 A; H=1-146. DR PDB; 1TWF; X-ray; 2.30 A; H=1-146. DR PDB; 1TWG; X-ray; 3.30 A; H=1-146. DR PDB; 1TWH; X-ray; 3.40 A; H=1-146. DR PDB; 1WCM; X-ray; 3.80 A; H=1-146. DR PDB; 1Y1V; X-ray; 3.80 A; H=1-146. DR PDB; 1Y1W; X-ray; 4.00 A; H=1-146. DR PDB; 1Y1Y; X-ray; 4.00 A; H=1-146. DR PDB; 1Y77; X-ray; 4.50 A; H=1-146. DR PDB; 24QP; EM; 2.73 A; H=1-146. DR PDB; 24QR; EM; 2.67 A; H=1-146. DR PDB; 24QS; EM; 2.74 A; H=1-146. DR PDB; 24QT; EM; 2.96 A; H=1-146. DR PDB; 2B63; X-ray; 3.80 A; H=1-146. DR PDB; 2B8K; X-ray; 4.15 A; H=1-146. DR PDB; 2E2H; X-ray; 3.95 A; H=1-146. DR PDB; 2E2I; X-ray; 3.41 A; H=1-146. DR PDB; 2E2J; X-ray; 3.50 A; H=1-146. DR PDB; 2JA5; X-ray; 3.80 A; H=1-146. DR PDB; 2JA6; X-ray; 4.00 A; H=1-146. DR PDB; 2JA7; X-ray; 3.80 A; H/T=1-146. DR PDB; 2JA8; X-ray; 3.80 A; H=1-146. DR PDB; 2NVQ; X-ray; 2.90 A; H=1-146. DR PDB; 2NVT; X-ray; 3.36 A; H=1-146. DR PDB; 2NVX; X-ray; 3.60 A; H=1-146. DR PDB; 2NVY; X-ray; 3.40 A; H=1-146. DR PDB; 2NVZ; X-ray; 4.30 A; H=1-146. DR PDB; 2R7Z; X-ray; 3.80 A; H=1-146. DR PDB; 2R92; X-ray; 3.80 A; H=1-146. DR PDB; 2R93; X-ray; 4.00 A; H=1-146. DR PDB; 2VUM; X-ray; 3.40 A; H=1-146. DR PDB; 2YU9; X-ray; 3.40 A; H=1-146. DR PDB; 3CQZ; X-ray; 2.80 A; H=1-146. DR PDB; 3FKI; X-ray; 3.88 A; H=1-146. DR PDB; 3GTG; X-ray; 3.78 A; H=1-146. DR PDB; 3GTJ; X-ray; 3.42 A; H=1-146. DR PDB; 3GTK; X-ray; 3.80 A; H=1-146. DR PDB; 3GTL; X-ray; 3.38 A; H=1-146. DR PDB; 3GTM; X-ray; 3.80 A; H=1-146. DR PDB; 3GTO; X-ray; 4.00 A; H=1-146. DR PDB; 3GTP; X-ray; 3.90 A; H=1-146. DR PDB; 3GTQ; X-ray; 3.80 A; H=1-146. DR PDB; 3H3V; X-ray; 4.00 A; I=1-146. DR PDB; 3HOU; X-ray; 3.20 A; H/T=1-146. DR PDB; 3HOV; X-ray; 3.50 A; H=1-146. DR PDB; 3HOW; X-ray; 3.60 A; H=1-146. DR PDB; 3HOX; X-ray; 3.65 A; H=1-146. DR PDB; 3HOY; X-ray; 3.40 A; H=1-146. DR PDB; 3HOZ; X-ray; 3.65 A; H=1-146. DR PDB; 3I4M; X-ray; 3.70 A; H=1-146. DR PDB; 3I4N; X-ray; 3.90 A; H=1-146. DR PDB; 3J0K; EM; 36.00 A; H=1-146. DR PDB; 3J1N; EM; 16.00 A; H=1-146. DR PDB; 3K1F; X-ray; 4.30 A; H=1-146. DR PDB; 3K7A; X-ray; 3.80 A; H=1-146. DR PDB; 3M3Y; X-ray; 3.18 A; H=1-146. DR PDB; 3M4O; X-ray; 3.57 A; H=1-146. DR PDB; 3PO2; X-ray; 3.30 A; H=1-146. DR PDB; 3PO3; X-ray; 3.30 A; H=1-146. DR PDB; 3QT1; X-ray; 4.30 A; H=1-146. DR PDB; 3RZD; X-ray; 3.30 A; H=1-146. DR PDB; 3RZO; X-ray; 3.00 A; H=1-146. DR PDB; 3S14; X-ray; 2.85 A; H=1-146. DR PDB; 3S15; X-ray; 3.30 A; H=1-146. DR PDB; 3S16; X-ray; 3.24 A; H=1-146. DR PDB; 3S17; X-ray; 3.20 A; H=1-146. DR PDB; 3S1M; X-ray; 3.13 A; H=1-146. DR PDB; 3S1N; X-ray; 3.10 A; H=1-146. DR PDB; 3S1Q; X-ray; 3.30 A; H=1-146. DR PDB; 3S1R; X-ray; 3.20 A; H=1-146. DR PDB; 3S2D; X-ray; 3.20 A; H=1-146. DR PDB; 3S2H; X-ray; 3.30 A; H=1-146. DR PDB; 4A3B; X-ray; 3.50 A; H=1-146. DR PDB; 4A3C; X-ray; 3.50 A; H=1-146. DR PDB; 4A3D; X-ray; 3.40 A; H=1-146. DR PDB; 4A3E; X-ray; 3.40 A; H=1-146. DR PDB; 4A3F; X-ray; 3.50 A; H=1-146. DR PDB; 4A3G; X-ray; 3.50 A; H=1-146. DR PDB; 4A3I; X-ray; 3.80 A; H=1-146. DR PDB; 4A3J; X-ray; 3.70 A; H=1-146. DR PDB; 4A3K; X-ray; 3.50 A; H=1-146. DR PDB; 4A3L; X-ray; 3.50 A; H=1-146. DR PDB; 4A3M; X-ray; 3.90 A; H=1-146. DR PDB; 4A93; X-ray; 3.40 A; H=1-146. DR PDB; 4BBR; X-ray; 3.40 A; H=1-146. DR PDB; 4BBS; X-ray; 3.60 A; H=1-146. DR PDB; 4BXX; X-ray; 3.28 A; H=1-146. DR PDB; 4BXZ; X-ray; 4.80 A; H=1-146. DR PDB; 4BY1; X-ray; 3.60 A; H=1-146. DR PDB; 4BY7; X-ray; 3.15 A; H=1-146. DR PDB; 4C2M; X-ray; 2.80 A; H/W=1-146. DR PDB; 4C3H; X-ray; 3.27 A; H=1-146. DR PDB; 4C3I; X-ray; 3.00 A; H=1-146. DR PDB; 4C3J; X-ray; 3.35 A; H=1-146. DR PDB; 4V1M; EM; 6.60 A; H=1-146. DR PDB; 4V1N; EM; 7.80 A; H=1-146. DR PDB; 4V1O; EM; 9.70 A; H=1-146. DR PDB; 4X67; X-ray; 4.10 A; H=1-146. DR PDB; 4X6A; X-ray; 3.96 A; H=1-146. DR PDB; 4Y52; X-ray; 3.50 A; H=1-146. DR PDB; 4Y7N; X-ray; 3.30 A; H=1-146. DR PDB; 4YM7; X-ray; 5.50 A; AH/BH/CH/DH/EH/FH=1-146. DR PDB; 5C3E; X-ray; 3.70 A; H=1-146. DR PDB; 5C44; X-ray; 3.95 A; H=1-146. DR PDB; 5C4A; X-ray; 4.20 A; H=1-146. DR PDB; 5C4J; X-ray; 4.00 A; H=1-146. DR PDB; 5C4X; X-ray; 4.00 A; H=1-146. DR PDB; 5FJ8; EM; 3.90 A; H=1-146. DR PDB; 5FJ9; EM; 4.60 A; H=1-146. DR PDB; 5FJA; EM; 4.65 A; H=1-146. DR PDB; 5FMF; EM; 6.00 A; H=1-146. DR PDB; 5FYW; EM; 4.35 A; H=1-146. DR PDB; 5FZ5; EM; 8.80 A; H=1-146. DR PDB; 5G5L; EM; 4.80 A; H=1-146. DR PDB; 5IP7; X-ray; 3.52 A; H=2-146. DR PDB; 5IP9; X-ray; 3.90 A; H=2-146. DR PDB; 5LMX; EM; 4.90 A; H=1-146. DR PDB; 5M3F; EM; 3.80 A; H=1-146. DR PDB; 5M3M; EM; 4.00 A; H=1-146. DR PDB; 5M5W; EM; 3.80 A; H=1-146. DR PDB; 5M5X; EM; 4.00 A; H=1-146. DR PDB; 5M5Y; EM; 4.00 A; H=1-146. DR PDB; 5M64; EM; 4.60 A; H=1-146. DR PDB; 5N5Y; EM; 7.70 A; H=1-146. DR PDB; 5N5Z; EM; 7.70 A; H=1-146. DR PDB; 5N60; EM; 7.70 A; H=1-146. DR PDB; 5N61; EM; 3.40 A; H=1-146. DR PDB; 5OA1; EM; 4.40 A; H=1-146. DR PDB; 5OQJ; EM; 4.70 A; H=1-146. DR PDB; 5OQM; EM; 5.80 A; H=1-146. DR PDB; 5OT2; X-ray; 3.20 A; H=1-146. DR PDB; 5SVA; EM; 15.30 A; H=1-146. DR PDB; 5U5Q; X-ray; 3.80 A; H=1-146. DR PDB; 5VVR; EM; 5.80 A; H=1-146. DR PDB; 5VVS; EM; 6.40 A; H=1-146. DR PDB; 5W4U; X-ray; 3.60 A; H=1-146. DR PDB; 5W51; X-ray; 3.40 A; H=1-146. DR PDB; 5W5Y; EM; 3.80 A; H=1-146. DR PDB; 5W64; EM; 4.20 A; H=1-146. DR PDB; 5W65; EM; 4.30 A; H=1-146. DR PDB; 5W66; EM; 3.90 A; H=1-146. DR PDB; 6BLO; X-ray; 3.40 A; H=1-146. DR PDB; 6BLP; X-ray; 3.20 A; H=1-146. DR PDB; 6BM2; X-ray; 3.40 A; H=1-146. DR PDB; 6BM4; X-ray; 2.95 A; H=1-146. DR PDB; 6BQF; X-ray; 3.35 A; H=1-146. DR PDB; 6CNB; EM; 4.10 A; H=1-146. DR PDB; 6CNC; EM; 4.10 A; H=1-146. DR PDB; 6CND; EM; 4.80 A; H=1-146. DR PDB; 6CNF; EM; 4.50 A; H=1-146. DR PDB; 6EU0; EM; 4.00 A; H=1-146. DR PDB; 6EU1; EM; 3.40 A; H=1-146. DR PDB; 6EU2; EM; 3.40 A; H=1-146. DR PDB; 6EU3; EM; 3.30 A; H=1-146. DR PDB; 6F40; EM; 3.70 A; H=1-146. DR PDB; 6F41; EM; 4.30 A; H=1-146. DR PDB; 6F42; EM; 5.50 A; H=1-146. DR PDB; 6F44; EM; 4.20 A; H=1-146. DR PDB; 6GYK; EM; 5.10 A; H=1-146. DR PDB; 6GYL; EM; 4.80 A; H=1-146. DR PDB; 6GYM; EM; 6.70 A; H=1-146. DR PDB; 6H67; EM; 3.60 A; H=1-146. DR PDB; 6H68; EM; 4.60 A; H=1-146. DR PDB; 6HKO; EM; 3.42 A; H=1-146. DR PDB; 6HLQ; EM; 3.18 A; H=1-146. DR PDB; 6HLR; EM; 3.18 A; H=1-146. DR PDB; 6HLS; EM; 3.21 A; H=1-146. DR PDB; 6I84; EM; 4.40 A; H=1-146. DR PDB; 6O6C; EM; 3.10 A; F=1-146. DR PDB; 6RQH; EM; 3.70 A; H=1-146. DR PDB; 6RQL; EM; 2.90 A; H=1-146. DR PDB; 6RQT; EM; 4.00 A; H=1-146. DR PDB; 6RRD; EM; 3.10 A; H=1-146. DR PDB; 6RUI; EM; 2.70 A; H=1-146. DR PDB; 6RUO; EM; 3.50 A; H=1-146. DR PDB; 6RWE; EM; 3.00 A; H=1-146. DR PDB; 6TPS; EM; 3.54 A; H=1-146. DR PDB; 6TUT; EM; 3.25 A; H=1-146. DR PDB; 6UPX; X-ray; 3.40 A; H=1-146. DR PDB; 6UPY; X-ray; 3.40 A; H=1-146. DR PDB; 6UPZ; X-ray; 3.10 A; H=1-146. DR PDB; 6UQ0; X-ray; 3.56 A; H=1-146. DR PDB; 6UQ1; X-ray; 3.60 A; H=1-146. DR PDB; 6UQ2; X-ray; 3.20 A; H=1-146. DR PDB; 6UQ3; X-ray; 3.47 A; H=1-146. DR PDB; 7KED; X-ray; 3.60 A; H=1-146. DR PDB; 7KEE; X-ray; 3.45 A; H=1-146. DR PDB; 7KEF; X-ray; 3.89 A; H=1-146. DR PDB; 7MEI; EM; 3.54 A; H/h=1-146. DR PDB; 7MK9; EM; 3.54 A; H=1-146. DR PDB; 7MKA; EM; 3.54 A; h=1-146. DR PDB; 7ML0; EM; 3.00 A; H=1-146. DR PDB; 7ML1; EM; 4.00 A; H=1-146. DR PDB; 7ML2; EM; 3.40 A; H=1-146. DR PDB; 7ML4; EM; 3.10 A; H=1-146. DR PDB; 7NKX; EM; 2.90 A; H=1-146. DR PDB; 7NKY; EM; 3.20 A; H=1-146. DR PDB; 7O4I; EM; 3.20 A; H=1-146. DR PDB; 7O4J; EM; 2.90 A; H=1-146. DR PDB; 7O72; EM; 3.40 A; H=1-146. DR PDB; 7O73; EM; 3.40 A; H=1-146. DR PDB; 7O75; EM; 3.20 A; H=1-146. DR PDB; 7RIM; X-ray; 2.90 A; H=1-146. DR PDB; 7RIP; X-ray; 3.30 A; H=1-146. DR PDB; 7RIQ; X-ray; 3.00 A; H=1-146. DR PDB; 7RIW; X-ray; 3.20 A; H=1-146. DR PDB; 7RIX; X-ray; 3.40 A; H=1-146. DR PDB; 7RIY; X-ray; 3.70 A; H=1-146. DR PDB; 7UI9; EM; 3.30 A; H=1-146. DR PDB; 7UIF; EM; 4.60 A; H=1-146. DR PDB; 7UIO; EM; 3.30 A; AH/BH=1-146. DR PDB; 7Z0H; EM; 2.60 A; H=1-146. DR PDB; 7Z1L; EM; 2.80 A; H=1-146. DR PDB; 7Z1M; EM; 3.40 A; H=1-146. DR PDB; 7Z1N; EM; 3.90 A; H=1-146. DR PDB; 7Z1O; EM; 2.70 A; H=1-146. DR PDB; 7Z2Z; EM; 3.07 A; H=1-146. DR PDB; 7Z30; EM; 2.90 A; H=1-146. DR PDB; 7Z31; EM; 2.76 A; H=1-146. DR PDB; 7ZS9; EM; 3.10 A; H=1-146. DR PDB; 7ZSA; EM; 4.00 A; H=1-146. DR PDB; 7ZSB; EM; 6.60 A; H=1-146. DR PDB; 8BWS; EM; 3.20 A; H=1-146. DR PDB; 8CEN; EM; 3.00 A; H=1-146. DR PDB; 8CEO; EM; 3.60 A; H=1-146. DR PDB; 8JCH; EM; 2.70 A; H=1-146. DR PDB; 8K5P; EM; 2.80 A; H=1-146. DR PDB; 8RAM; EM; 2.80 A; H=1-146. DR PDB; 8RAP; EM; 4.30 A; H=1-146. DR PDB; 8TUG; EM; 3.50 A; H=1-146. DR PDB; 8TVP; EM; 3.70 A; H=1-146. DR PDB; 8TVQ; EM; 4.60 A; H=1-146. DR PDB; 8TVS; EM; 4.40 A; H=1-146. DR PDB; 8TVV; EM; 3.70 A; H=1-146. DR PDB; 8TVW; EM; 3.60 A; H=1-146. DR PDB; 8TVX; EM; 3.70 A; H=1-146. DR PDB; 8TVY; EM; 3.10 A; H=1-146. DR PDB; 8UKQ; X-ray; 3.50 A; H=1-146. DR PDB; 8UKR; X-ray; 3.78 A; H=1-146. DR PDB; 8UKS; X-ray; 3.40 A; H=1-146. DR PDB; 8UKT; X-ray; 3.60 A; H=1-146. DR PDB; 8UKU; X-ray; 3.60 A; H=1-146. DR PDB; 8UMH; EM; 4.10 A; H=1-146. DR PDB; 8UMI; EM; 3.70 A; H=1-146. DR PDB; 8UOQ; EM; 3.80 A; H=1-146. DR PDB; 8UOT; EM; 3.70 A; H=1-146. DR PDB; 9BVT; X-ray; 3.40 A; H=1-146. DR PDB; 9BW0; X-ray; 3.51 A; H=1-146. DR PDB; 9G1V; EM; 2.70 A; H=1-146. DR PDB; 9G1X; EM; 3.50 A; H=1-146. DR PDB; 9G23; EM; 3.40 A; H=1-146. DR PDB; 9G24; EM; 3.50 A; H=1-146. DR PDB; 9G26; EM; 3.40 A; H=1-146. DR PDB; 9G27; EM; 2.80 A; H=1-146. DR PDB; 9G29; EM; 3.30 A; H=1-146. DR PDB; 9G2B; EM; 3.20 A; H=1-146. DR PDB; 9G2C; EM; 3.50 A; H=1-146. DR PDB; 9JA1; EM; 2.98 A; H=1-146. DR PDB; 9K7F; EM; 2.50 A; H=1-146. DR PDB; 9KD7; EM; 3.09 A; H=1-146. DR PDB; 9KD8; EM; 2.46 A; H=1-146. DR PDB; 9KD9; EM; 2.88 A; H=1-146. DR PDB; 9KDN; EM; 2.96 A; H=1-146. DR PDB; 9KDO; EM; 2.92 A; H=1-146. DR PDB; 9KDQ; EM; 2.63 A; H=1-146. DR PDB; 9N5B; X-ray; 3.10 A; H=1-146. DR PDB; 9N5C; X-ray; 3.60 A; H=1-146. DR PDB; 9N5D; X-ray; 3.35 A; H=1-146. DR PDB; 9N5E; X-ray; 3.75 A; H=1-146. DR PDB; 9N5F; X-ray; 3.60 A; H=1-146. DR PDB; 9N5G; X-ray; 3.15 A; H=1-146. DR PDB; 9PVV; X-ray; 3.48 A; H=1-146. DR PDB; 9PVW; X-ray; 3.56 A; H=1-146. DR PDB; 9PVX; X-ray; 3.39 A; H=1-146. DR PDB; 9QEB; EM; 2.26 A; H=1-146. DR PDB; 9RYB; EM; 2.33 A; H=1-146. DR PDB; 9SAY; EM; 3.44 A; H=1-146. DR PDB; 9SB1; EM; 2.98 A; H=1-146. DR PDB; 9SB3; EM; 3.05 A; H=1-146. DR PDB; 9SV6; EM; 1.96 A; H=1-146. DR PDB; 9W8R; EM; 2.68 A; H=1-146. DR PDB; 9W8T; EM; 2.56 A; H=1-146. DR PDB; 9W8U; EM; 2.61 A; H=1-146. DR PDB; 9W8V; EM; 2.23 A; H=1-146. DR PDB; 9W8W; EM; 2.91 A; H=1-146. DR PDB; 9W8X; EM; 2.86 A; H=1-146. DR PDB; 9W8Y; EM; 3.08 A; H=1-146. DR PDB; 9W8Z; EM; 3.03 A; H=1-146. DR PDB; 9WQ7; EM; 2.72 A; H=1-146. DR PDB; 9WQ8; EM; 2.98 A; H=1-146. DR PDB; 9WQ9; EM; 2.95 A; H=1-146. DR AlphaFoldDB; P20436; -. DR EMDB; EMD-0090; -. DR EMDB; EMD-0091; -. DR EMDB; EMD-0092; -. DR EMDB; EMD-0146; -. DR EMDB; EMD-0147; -. DR EMDB; EMD-0238; -. DR EMDB; EMD-0239; -. DR EMDB; EMD-0240; -. DR EMDB; EMD-0241; -. DR EMDB; EMD-0633; -. DR EMDB; EMD-10006; -. DR EMDB; EMD-10007; -. DR EMDB; EMD-10038; -. DR EMDB; EMD-10544; -. DR EMDB; EMD-10595; -. DR EMDB; EMD-12449; -. DR EMDB; EMD-12450; -. DR EMDB; EMD-12719; -. DR EMDB; EMD-12720; -. DR EMDB; EMD-12743; -. DR EMDB; EMD-12744; -. DR EMDB; EMD-12745; -. DR EMDB; EMD-14421; -. DR EMDB; EMD-14447; -. DR EMDB; EMD-14448; -. DR EMDB; EMD-14449; -. DR EMDB; EMD-14451; -. DR EMDB; EMD-14468; -. DR EMDB; EMD-14469; -. DR EMDB; EMD-14470; -. DR EMDB; EMD-14927; -. DR EMDB; EMD-14928; -. DR EMDB; EMD-14929; -. DR EMDB; EMD-16299; -. DR EMDB; EMD-16610; -. DR EMDB; EMD-16611; -. DR EMDB; EMD-19019; -. DR EMDB; EMD-19022; -. DR EMDB; EMD-26542; -. DR EMDB; EMD-26544; -. DR EMDB; EMD-26551; -. DR EMDB; EMD-2784; -. DR EMDB; EMD-2785; -. DR EMDB; EMD-2786; -. DR EMDB; EMD-3446; -. DR EMDB; EMD-3447; -. DR EMDB; EMD-3448; -. DR EMDB; EMD-3449; -. DR EMDB; EMD-3590; -. DR EMDB; EMD-3591; -. DR EMDB; EMD-3592; -. DR EMDB; EMD-3593; -. DR EMDB; EMD-36162; -. DR EMDB; EMD-36908; -. DR EMDB; EMD-3727; -. DR EMDB; EMD-3846; -. DR EMDB; EMD-3850; -. DR EMDB; EMD-3955; -. DR EMDB; EMD-3956; -. DR EMDB; EMD-3957; -. DR EMDB; EMD-3958; -. DR EMDB; EMD-4088; -. DR EMDB; EMD-4147; -. DR EMDB; EMD-4148; -. DR EMDB; EMD-4180; -. DR EMDB; EMD-4181; -. DR EMDB; EMD-4182; -. DR EMDB; EMD-4183; -. DR EMDB; EMD-42437; -. DR EMDB; EMD-42438; -. DR EMDB; EMD-4429; -. DR EMDB; EMD-4982; -. DR EMDB; EMD-4984; -. DR EMDB; EMD-4985; -. DR EMDB; EMD-4987; -. DR EMDB; EMD-50955; -. DR EMDB; EMD-50956; -. DR EMDB; EMD-50962; -. DR EMDB; EMD-50963; -. DR EMDB; EMD-50965; -. DR EMDB; EMD-50966; -. DR EMDB; EMD-50970; -. DR EMDB; EMD-50971; -. DR EMDB; EMD-50972; -. DR EMDB; EMD-53053; -. DR EMDB; EMD-54374; -. DR EMDB; EMD-54708; -. DR EMDB; EMD-54710; -. DR EMDB; EMD-54712; -. DR EMDB; EMD-54713; -. DR EMDB; EMD-54730; -. DR EMDB; EMD-54731; -. DR EMDB; EMD-54732; -. DR EMDB; EMD-54733; -. DR EMDB; EMD-54734; -. DR EMDB; EMD-54735; -. DR EMDB; EMD-54736; -. DR EMDB; EMD-54737; -. DR EMDB; EMD-54738; -. DR EMDB; EMD-54739; -. DR EMDB; EMD-54740; -. DR EMDB; EMD-54741; -. DR EMDB; EMD-54742; -. DR EMDB; EMD-54743; -. DR EMDB; EMD-54744; -. DR EMDB; EMD-54745; -. DR EMDB; EMD-54746; -. DR EMDB; EMD-54747; -. DR EMDB; EMD-54748; -. DR EMDB; EMD-54749; -. DR EMDB; EMD-55239; -. DR EMDB; EMD-57322; -. DR EMDB; EMD-57673; -. DR EMDB; EMD-57676; -. DR EMDB; EMD-61287; -. DR EMDB; EMD-62148; -. DR EMDB; EMD-62264; -. DR EMDB; EMD-62265; -. DR EMDB; EMD-62266; -. DR EMDB; EMD-62282; -. DR EMDB; EMD-62283; -. DR EMDB; EMD-62284; -. DR EMDB; EMD-65749; -. DR EMDB; EMD-65751; -. DR EMDB; EMD-65752; -. DR EMDB; EMD-65753; -. DR EMDB; EMD-65754; -. DR EMDB; EMD-65755; -. DR EMDB; EMD-65756; -. DR EMDB; EMD-65757; -. DR EMDB; EMD-66161; -. DR EMDB; EMD-66162; -. DR EMDB; EMD-66163; -. DR EMDB; EMD-69770; -. DR EMDB; EMD-69771; -. DR EMDB; EMD-69772; -. DR EMDB; EMD-69773; -. DR EMDB; EMD-7530; -. DR EMDB; EMD-7531; -. DR EMDB; EMD-7532; -. DR EMDB; EMD-7533; -. DR EMDB; EMD-8305; -. DR EMDB; EMD-8735; -. DR EMDB; EMD-8737; -. DR EMDB; EMD-8771; -. DR EMDB; EMD-8773; -. DR EMDB; EMD-8774; -. DR EMDB; EMD-8775; -. DR EMDB; EMD-8776; -. DR EMDB; EMD-8777; -. DR SMR; P20436; -. DR BioGRID; 34618; 254. 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-2195N; -. DR FunCoup; P20436; 991. DR IntAct; P20436; 51. DR STRING; 4932.YOR224C; -. DR iPTMnet; P20436; -. DR PaxDb; 4932-YOR224C; -. DR PeptideAtlas; P20436; -. DR EnsemblFungi; YOR224C_mRNA; YOR224C; YOR224C. DR GeneID; 854399; -. DR KEGG; sce:YOR224C; -. DR AGR; SGD:S000005750; -. DR SGD; S000005750; RPB8. DR VEuPathDB; FungiDB:YOR224C; -. DR eggNOG; KOG3400; Eukaryota. DR HOGENOM; CLU_103864_1_0_1; -. DR InParanoid; P20436; -. DR OMA; AASYEYI; -. DR OrthoDB; 20018at2759; -. DR BioCyc; YEAST:G3O-33723-MONOMER; -. 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-72203; Processing of Capped Intron-Containing Pre-mRNA. 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-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 BioGRID-ORCS; 854399; 10 hits in 10 CRISPR screens. DR CD-CODE; BDAE0F88; Nucleolus. DR EvolutionaryTrace; P20436; -. DR PRO; PR:P20436; -. DR Proteomes; UP000002311; Chromosome XV. DR RNAct; P20436; protein. 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:0003899; F:DNA-directed RNA polymerase activity; IDA:UniProtKB. DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal. DR GO; GO:0001172; P:RNA-templated transcription; IEA:GOC. 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; IPI:SGD. DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:ComplexPortal. DR GO; GO:0006362; P:transcription elongation by RNA polymerase I; IDA:ComplexPortal. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0006361; P:transcription initiation at RNA polymerase I promoter; IDA:ComplexPortal. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:ComplexPortal. DR GO; GO:0006384; P:transcription initiation at RNA polymerase III promoter; IDA:ComplexPortal. DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IDA:SGD. DR FunFam; 2.40.50.140:FF:000191; DNA-directed RNA polymerases I, II, and III subunit RPABC3; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR005570; RPABC3. DR PANTHER; PTHR10917; DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC3; 1. DR PANTHER; PTHR10917:SF0; DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC3; 1. DR Pfam; PF03870; RNA_pol_Rpb8; 1. DR PIRSF; PIRSF000779; RNA_pol_Rpb8; 1. DR SMART; SM00658; RPOL8c; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; DNA-binding; DNA-directed RNA polymerase; KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis; KW Transcription. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..146 FT /note="DNA-directed RNA polymerases I, II, and III subunit FT RPABC3" FT /id="PRO_0000074001" FT REGION 16..39 FT /note="Non-specific ssDNA binding" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 68 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18407956" FT STRAND 4..6 FT /evidence="ECO:0007829|PDB:6RUO" FT STRAND 7..16 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 21..32 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 37..43 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 54..58 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:9KD9" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:8JCH" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:8TVY" FT HELIX 78..81 FT /evidence="ECO:0007829|PDB:2NVQ" FT TURN 84..86 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 89..92 FT /evidence="ECO:0007829|PDB:9KD8" FT STRAND 93..101 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 108..110 FT /evidence="ECO:0007829|PDB:8JCH" FT STRAND 112..118 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 121..128 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 129..133 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 140..145 FT /evidence="ECO:0007829|PDB:1TWF" SQ SEQUENCE 146 AA; 16511 MW; 5B71693FE6FD8863 CRC64; MSNTLFDDIF QVSEVDPGRY NKVCRIEAAS TTQDQCKLTL DINVELFPVA AQDSLTVTIA SSLNLEDTPA NDSSATRSWR PPQAGDRSLA DDYDYVMYGT AYKFEEVSKD LIAVYYSFGG LLMRLEGNYR NLNNLKQENA YLLIRR //