ID RPB3_YEAST Reviewed; 318 AA. AC P16370; D6VVQ8; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 27-MAR-2024, entry version 225. DE RecName: Full=DNA-directed RNA polymerase II subunit RPB3; DE Short=RNA polymerase II subunit 3; DE Short=RNA polymerase II subunit B3; DE AltName: Full=B44.5; DE AltName: Full=DNA-directed RNA polymerase II 45 kDa polypeptide; GN Name=RPB3; OrderedLocusNames=YIL021W; 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], AND PROTEIN SEQUENCE OF 206-223. RX PubMed=2685562; DOI=10.1128/mcb.9.12.5387-5394.1989; RA Kolodziej P., Young R.A.; RT "RNA polymerase II subunit RPB3 is an essential component of the mRNA RT transcription apparatus."; RL Mol. Cell. Biol. 9:5387-5394(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169870; RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C., RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., RA Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."; RL Nature 387:84-87(1997). RN [3] 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 [4] 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 [5] RP FUNCTION, AND MUTAGENESIS OF LYS-9. RX PubMed=16537912; DOI=10.1128/mcb.26.7.2688-2696.2006; RA Steinmetz E.J., Ng S.B., Cloute J.P., Brow D.A.; RT "cis- and trans-Acting determinants of transcription termination by yeast RT RNA polymerase II."; RL Mol. Cell. Biol. 26:2688-2696(2006). RN [6] 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 [7] 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 [8] 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 [9] 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 [10] 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 [11] 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 [12] 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 [13] 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 [14] 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 [15] 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 [16] 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 [17] 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 [18] 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 [19] 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). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC Component of RNA polymerase II which synthesizes mRNA precursors and CC many functional non-coding RNAs. Pol II is the central component of the CC basal RNA polymerase II transcription machinery. It is composed of CC mobile elements that move relative to each other. RPB3 is part of the CC core element with the central large cleft and the clamp element that CC moves to open and close the cleft. Seems to be involved in CC transcription termination. {ECO:0000269|PubMed:16537912}. CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting CC of 12 subunits. {ECO:0000269|PubMed:11805306, CC ECO:0000269|PubMed:12914699, ECO:0000269|PubMed:16341226}. CC -!- INTERACTION: CC P16370; P38902: RPB11; NbExp=4; IntAct=EBI-15773, EBI-15806; CC P16370; P08518: RPB2; NbExp=5; IntAct=EBI-15773, EBI-15767; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: Present with 10000 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase CC subunit 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; Z46881; CAA86971.1; -; Genomic_DNA. DR EMBL; M27496; AAA34889.1; -; Genomic_DNA. DR EMBL; BK006942; DAA08524.1; -; Genomic_DNA. DR PIR; S49961; S49961. DR RefSeq; NP_012243.3; NM_001179371.3. DR PDB; 1I3Q; X-ray; 3.10 A; C=1-318. DR PDB; 1I50; X-ray; 2.80 A; C=1-318. DR PDB; 1I6H; X-ray; 3.30 A; C=1-318. DR PDB; 1K83; X-ray; 2.80 A; C=1-318. DR PDB; 1NIK; X-ray; 4.10 A; C=1-318. DR PDB; 1NT9; X-ray; 4.20 A; C=1-318. DR PDB; 1PQV; X-ray; 3.80 A; C=1-318. DR PDB; 1R5U; X-ray; 4.50 A; C=1-318. DR PDB; 1R9S; X-ray; 4.25 A; C=1-318. DR PDB; 1R9T; X-ray; 3.50 A; C=1-318. DR PDB; 1SFO; X-ray; 3.61 A; C=1-318. DR PDB; 1TWA; X-ray; 3.20 A; C=1-318. DR PDB; 1TWC; X-ray; 3.00 A; C=1-318. DR PDB; 1TWF; X-ray; 2.30 A; C=1-318. DR PDB; 1TWG; X-ray; 3.30 A; C=1-318. DR PDB; 1TWH; X-ray; 3.40 A; C=1-318. DR PDB; 1WCM; X-ray; 3.80 A; C=1-318. DR PDB; 1Y1V; X-ray; 3.80 A; C=1-318. DR PDB; 1Y1W; X-ray; 4.00 A; C=1-318. DR PDB; 1Y1Y; X-ray; 4.00 A; C=1-318. DR PDB; 1Y77; X-ray; 4.50 A; C=1-318. DR PDB; 2B63; X-ray; 3.80 A; C=1-318. DR PDB; 2B8K; X-ray; 4.15 A; C=1-318. DR PDB; 2E2H; X-ray; 3.95 A; C=1-318. DR PDB; 2E2I; X-ray; 3.41 A; C=1-318. DR PDB; 2E2J; X-ray; 3.50 A; C=1-318. DR PDB; 2JA5; X-ray; 3.80 A; C=1-318. DR PDB; 2JA6; X-ray; 4.00 A; C=1-318. DR PDB; 2JA7; X-ray; 3.80 A; C/O=1-318. DR PDB; 2JA8; X-ray; 3.80 A; C=1-318. DR PDB; 2NVQ; X-ray; 2.90 A; C=1-318. DR PDB; 2NVT; X-ray; 3.36 A; C=1-318. DR PDB; 2NVX; X-ray; 3.60 A; C=1-318. DR PDB; 2NVY; X-ray; 3.40 A; C=1-318. DR PDB; 2NVZ; X-ray; 4.30 A; C=1-318. DR PDB; 2R7Z; X-ray; 3.80 A; C=1-318. DR PDB; 2R92; X-ray; 3.80 A; C=1-318. DR PDB; 2R93; X-ray; 4.00 A; C=1-318. DR PDB; 2VUM; X-ray; 3.40 A; C=1-318. DR PDB; 2YU9; X-ray; 3.40 A; C=1-318. DR PDB; 3CQZ; X-ray; 2.80 A; C=1-318. DR PDB; 3FKI; X-ray; 3.88 A; C=1-318. DR PDB; 3GTG; X-ray; 3.78 A; C=1-318. DR PDB; 3GTJ; X-ray; 3.42 A; C=1-318. DR PDB; 3GTK; X-ray; 3.80 A; C=1-318. DR PDB; 3GTL; X-ray; 3.38 A; C=1-318. DR PDB; 3GTM; X-ray; 3.80 A; C=1-318. DR PDB; 3GTO; X-ray; 4.00 A; C=1-318. DR PDB; 3GTP; X-ray; 3.90 A; C=1-318. DR PDB; 3GTQ; X-ray; 3.80 A; C=1-318. DR PDB; 3H3V; X-ray; 4.00 A; D=1-318. DR PDB; 3HOU; X-ray; 3.20 A; C/O=1-318. DR PDB; 3HOV; X-ray; 3.50 A; C=1-318. DR PDB; 3HOW; X-ray; 3.60 A; C=2-318. DR PDB; 3HOX; X-ray; 3.65 A; C=2-318. DR PDB; 3HOY; X-ray; 3.40 A; C=2-318. DR PDB; 3HOZ; X-ray; 3.65 A; C=2-318. DR PDB; 3I4M; X-ray; 3.70 A; C=1-318. DR PDB; 3I4N; X-ray; 3.90 A; C=1-318. DR PDB; 3J0K; EM; 36.00 A; C=1-268. DR PDB; 3J1N; EM; 16.00 A; C=1-268. DR PDB; 3K1F; X-ray; 4.30 A; C=1-318. DR PDB; 3K7A; X-ray; 3.80 A; C=1-318. DR PDB; 3M3Y; X-ray; 3.18 A; C=1-318. DR PDB; 3M4O; X-ray; 3.57 A; C=1-318. DR PDB; 3PO2; X-ray; 3.30 A; C=1-318. DR PDB; 3PO3; X-ray; 3.30 A; C=1-318. DR PDB; 3QT1; X-ray; 4.30 A; C=1-318. DR PDB; 3RZD; X-ray; 3.30 A; C=1-318. DR PDB; 3RZO; X-ray; 3.00 A; C=1-318. DR PDB; 3S14; X-ray; 2.85 A; C=1-318. DR PDB; 3S15; X-ray; 3.30 A; C=1-318. DR PDB; 3S16; X-ray; 3.24 A; C=1-318. DR PDB; 3S17; X-ray; 3.20 A; C=1-318. DR PDB; 3S1M; X-ray; 3.13 A; C=1-318. DR PDB; 3S1N; X-ray; 3.10 A; C=1-318. DR PDB; 3S1Q; X-ray; 3.30 A; C=1-318. DR PDB; 3S1R; X-ray; 3.20 A; C=1-318. DR PDB; 3S2D; X-ray; 3.20 A; C=1-318. DR PDB; 3S2H; X-ray; 3.30 A; C=1-318. DR PDB; 4A3B; X-ray; 3.50 A; C=1-318. DR PDB; 4A3C; X-ray; 3.50 A; C=1-318. DR PDB; 4A3D; X-ray; 3.40 A; C=1-318. DR PDB; 4A3E; X-ray; 3.40 A; C=1-318. DR PDB; 4A3F; X-ray; 3.50 A; C=1-318. DR PDB; 4A3G; X-ray; 3.50 A; C=1-318. DR PDB; 4A3I; X-ray; 3.80 A; C=1-318. DR PDB; 4A3J; X-ray; 3.70 A; C=1-318. DR PDB; 4A3K; X-ray; 3.50 A; C=1-318. DR PDB; 4A3L; X-ray; 3.50 A; C=1-318. DR PDB; 4A3M; X-ray; 3.90 A; C=1-318. DR PDB; 4A93; X-ray; 3.40 A; C=1-318. DR PDB; 4BBR; X-ray; 3.40 A; C=1-318. DR PDB; 4BBS; X-ray; 3.60 A; C=1-318. DR PDB; 4BXX; X-ray; 3.28 A; C=1-318. DR PDB; 4BXZ; X-ray; 4.80 A; C=1-318. DR PDB; 4BY1; X-ray; 3.60 A; C=1-318. DR PDB; 4BY7; X-ray; 3.15 A; C=1-318. DR PDB; 4V1M; EM; 6.60 A; C=1-318. DR PDB; 4V1N; EM; 7.80 A; C=1-318. DR PDB; 4V1O; EM; 9.70 A; C=1-318. DR PDB; 4X67; X-ray; 4.10 A; C=1-318. DR PDB; 4X6A; X-ray; 3.96 A; C=1-318. DR PDB; 4Y52; X-ray; 3.50 A; C=1-318. DR PDB; 4Y7N; X-ray; 3.30 A; C=1-318. DR PDB; 5C3E; X-ray; 3.70 A; C=1-318. DR PDB; 5C44; X-ray; 3.95 A; C=1-318. DR PDB; 5C4A; X-ray; 4.20 A; C=1-318. DR PDB; 5C4J; X-ray; 4.00 A; C=1-318. DR PDB; 5C4X; X-ray; 4.00 A; C=1-318. DR PDB; 5FMF; EM; 6.00 A; C=3-268. DR PDB; 5FYW; EM; 4.35 A; C=1-318. DR PDB; 5FZ5; EM; 8.80 A; C=1-318. DR PDB; 5IP7; X-ray; 3.52 A; C=3-268. DR PDB; 5IP9; X-ray; 3.90 A; C=3-268. DR PDB; 5OQJ; EM; 4.70 A; C=1-318. DR PDB; 5OQM; EM; 5.80 A; C=1-318. DR PDB; 5OT2; X-ray; 3.20 A; C=1-318. DR PDB; 5SVA; EM; 15.30 A; C=1-318. DR PDB; 5U5Q; X-ray; 3.80 A; C=1-318. DR PDB; 5VVR; EM; 5.80 A; C=1-318. DR PDB; 5VVS; EM; 6.40 A; C=1-318. DR PDB; 5W4U; X-ray; 3.60 A; C=1-318. DR PDB; 5W51; X-ray; 3.40 A; C=1-318. DR PDB; 6BLO; X-ray; 3.40 A; C=1-318. DR PDB; 6BLP; X-ray; 3.20 A; C=1-318. DR PDB; 6BM2; X-ray; 3.40 A; C=1-318. DR PDB; 6BM4; X-ray; 2.95 A; C=1-318. DR PDB; 6BQF; X-ray; 3.35 A; C=1-318. DR PDB; 6GYK; EM; 5.10 A; C=1-318. DR PDB; 6GYL; EM; 4.80 A; C=1-318. DR PDB; 6GYM; EM; 6.70 A; C=1-318. DR PDB; 6I84; EM; 4.40 A; C=1-318. DR PDB; 6O6C; EM; 3.10 A; C=1-318. DR PDB; 6UPX; X-ray; 3.40 A; C=1-318. DR PDB; 6UPY; X-ray; 3.40 A; C=1-318. DR PDB; 6UPZ; X-ray; 3.10 A; C=1-318. DR PDB; 6UQ0; X-ray; 3.56 A; C=1-318. DR PDB; 6UQ1; X-ray; 3.60 A; C=1-318. DR PDB; 6UQ2; X-ray; 3.20 A; C=1-318. DR PDB; 6UQ3; X-ray; 3.47 A; C=1-318. DR PDB; 7KED; X-ray; 3.60 A; C=1-318. DR PDB; 7KEE; X-ray; 3.45 A; C=1-318. DR PDB; 7KEF; X-ray; 3.89 A; C=1-318. DR PDB; 7MEI; EM; 3.54 A; C/c=1-318. DR PDB; 7MK9; EM; 3.54 A; C=1-318. DR PDB; 7MKA; EM; 3.54 A; c=1-318. DR PDB; 7ML0; EM; 3.00 A; C=1-318. DR PDB; 7ML1; EM; 4.00 A; C=1-318. DR PDB; 7ML2; EM; 3.40 A; C=1-318. DR PDB; 7ML4; EM; 3.10 A; C=1-318. DR PDB; 7NKX; EM; 2.90 A; C=1-318. DR PDB; 7NKY; EM; 3.20 A; C=1-318. DR PDB; 7O4I; EM; 3.20 A; C=4-318. DR PDB; 7O4J; EM; 2.90 A; C=4-318. DR PDB; 7O72; EM; 3.40 A; C=4-318. DR PDB; 7O73; EM; 3.40 A; C=4-318. DR PDB; 7O75; EM; 3.20 A; C=4-318. DR PDB; 7RIM; X-ray; 2.90 A; C=1-318. DR PDB; 7RIP; X-ray; 3.30 A; C=1-318. DR PDB; 7RIQ; X-ray; 3.00 A; C=1-318. DR PDB; 7RIW; X-ray; 3.20 A; C=1-318. DR PDB; 7RIX; X-ray; 3.40 A; C=1-318. DR PDB; 7RIY; X-ray; 3.70 A; C=1-318. DR PDB; 7UI9; EM; 3.30 A; C=1-318. DR PDB; 7UIF; EM; 4.60 A; C=1-318. DR PDB; 7UIO; EM; 3.30 A; AC/BC=1-318. DR PDB; 7ZS9; EM; 3.10 A; C=4-318. DR PDB; 7ZSA; EM; 4.00 A; C=4-318. DR PDB; 7ZSB; EM; 6.60 A; C=4-318. DR PDB; 8CEN; EM; 3.00 A; C=4-318. DR PDB; 8CEO; EM; 3.60 A; C=4-318. 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; 4V1M; -. DR PDBsum; 4V1N; -. DR PDBsum; 4V1O; -. DR PDBsum; 4X67; -. DR PDBsum; 4X6A; -. DR PDBsum; 4Y52; -. DR PDBsum; 4Y7N; -. DR PDBsum; 5C3E; -. DR PDBsum; 5C44; -. DR PDBsum; 5C4A; -. DR PDBsum; 5C4J; -. DR PDBsum; 5C4X; -. DR PDBsum; 5FMF; -. DR PDBsum; 5FYW; -. DR PDBsum; 5FZ5; -. DR PDBsum; 5IP7; -. DR PDBsum; 5IP9; -. 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; 6BLO; -. DR PDBsum; 6BLP; -. DR PDBsum; 6BM2; -. DR PDBsum; 6BM4; -. DR PDBsum; 6BQF; -. DR PDBsum; 6GYK; -. DR PDBsum; 6GYL; -. DR PDBsum; 6GYM; -. DR PDBsum; 6I84; -. DR PDBsum; 6O6C; -. 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; 7MEI; -. DR PDBsum; 7MK9; -. DR PDBsum; 7MKA; -. DR PDBsum; 7ML0; -. DR PDBsum; 7ML1; -. DR PDBsum; 7ML2; -. DR PDBsum; 7ML4; -. DR PDBsum; 7NKX; -. DR PDBsum; 7NKY; -. DR PDBsum; 7O4I; -. DR PDBsum; 7O4J; -. 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 PDBsum; 7UI9; -. DR PDBsum; 7UIF; -. DR PDBsum; 7UIO; -. DR PDBsum; 7ZS9; -. DR PDBsum; 7ZSA; -. DR PDBsum; 7ZSB; -. DR PDBsum; 8CEN; -. DR PDBsum; 8CEO; -. DR AlphaFoldDB; P16370; -. DR EMDB; EMD-0090; -. DR EMDB; EMD-0091; -. DR EMDB; EMD-0092; -. DR EMDB; EMD-0633; -. 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-14927; -. DR EMDB; EMD-14928; -. DR EMDB; EMD-14929; -. DR EMDB; EMD-23789; -. DR EMDB; EMD-23904; -. DR EMDB; EMD-23905; -. DR EMDB; EMD-23906; -. DR EMDB; EMD-23908; -. 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-3846; -. DR EMDB; EMD-3850; -. DR EMDB; EMD-4429; -. DR EMDB; EMD-8305; -. DR EMDB; EMD-8735; -. DR EMDB; EMD-8737; -. DR SMR; P16370; -. DR BioGRID; 34967; 911. DR ComplexPortal; CPX-2662; DNA-directed RNA polymerase II complex. DR DIP; DIP-837N; -. DR IntAct; P16370; 41. DR MINT; P16370; -. DR STRING; 4932.YIL021W; -. DR iPTMnet; P16370; -. DR MaxQB; P16370; -. DR PaxDb; 4932-YIL021W; -. DR PeptideAtlas; P16370; -. DR EnsemblFungi; YIL021W_mRNA; YIL021W; YIL021W. DR GeneID; 854791; -. DR KEGG; sce:YIL021W; -. DR AGR; SGD:S000001283; -. DR SGD; S000001283; RPB3. DR VEuPathDB; FungiDB:YIL021W; -. DR eggNOG; KOG1522; Eukaryota. DR GeneTree; ENSGT00950000183100; -. DR HOGENOM; CLU_038421_1_1_1; -. DR InParanoid; P16370; -. DR OMA; PENIVMM; -. DR OrthoDB; 5472982at2759; -. DR BioCyc; YEAST:G3O-31296-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-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-77075; RNA Pol II CTD phosphorylation and interaction with CE. DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression. DR BioGRID-ORCS; 854791; 2 hits in 10 CRISPR screens. DR EvolutionaryTrace; P16370; -. DR PRO; PR:P16370; -. DR Proteomes; UP000002311; Chromosome IX. DR RNAct; P16370; Protein. DR GO; GO:0005654; C:nucleoplasm; IDA:SGD. DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal. DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:SGD. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0001172; P:RNA-templated transcription; IEA:GOC. DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IMP:SGD. DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:SGD. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:ComplexPortal. DR CDD; cd07031; RNAP_II_RPB3; 1. DR Gene3D; 2.170.120.12; DNA-directed RNA polymerase, insert domain; 1. DR Gene3D; 3.30.1360.10; RNA polymerase, RBP11-like subunit; 1. DR HAMAP; MF_00320; RNApol_arch_Rpo3; 1. DR InterPro; IPR001514; DNA-dir_RNA_pol_30-40kDasu_CS. DR InterPro; IPR011262; DNA-dir_RNA_pol_insert. DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3. DR InterPro; IPR036603; RBP11-like. DR InterPro; IPR022842; RNAP_Rpo3/Rpb3/RPAC1. DR InterPro; IPR036643; RNApol_insert_sf. DR PANTHER; PTHR11800; DNA-DIRECTED RNA POLYMERASE; 1. DR PANTHER; PTHR11800:SF2; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB3; 1. DR Pfam; PF01000; RNA_pol_A_bac; 1. DR Pfam; PF01193; RNA_pol_L; 1. DR SMART; SM00662; RPOLD; 1. DR SUPFAM; SSF56553; Insert subdomain of RNA polymerase alpha subunit; 1. DR SUPFAM; SSF55257; RBP11-like subunits of RNA polymerase; 1. DR PROSITE; PS00446; RNA_POL_D_30KD; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; KW DNA-directed RNA polymerase; Metal-binding; Nucleus; Reference proteome; KW Transcription; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..318 FT /note="DNA-directed RNA polymerase II subunit RPB3" FT /id="PRO_0000132748" FT REGION 297..318 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 86 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 88 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 92 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT VARIANT 30 FT /note="A -> D (in mutant RPB3-1)" FT MUTAGEN 9 FT /note="K->E: Transcript termination readthrough." FT /evidence="ECO:0000269|PubMed:16537912" FT CONFLICT 175 FT /note="A -> G (in Ref. 1; AAA34889)" FT /evidence="ECO:0000305" FT STRAND 5..7 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:3CQZ" FT STRAND 15..18 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 21..25 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 27..39 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 43..54 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 60..68 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 77..79 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 83..85 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 86..90 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 93..95 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 96..104 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 111..114 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 115..117 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 128..132 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:3S14" FT STRAND 142..147 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 152..162 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 164..166 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 173..180 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 182..186 FT /evidence="ECO:0007829|PDB:7NKX" FT HELIX 197..200 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 208..210 FT /evidence="ECO:0007829|PDB:7RIM" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 228..234 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 240..265 FT /evidence="ECO:0007829|PDB:1TWF" SQ SEQUENCE 318 AA; 35298 MW; 8E1D1E6BB7B51D89 CRC64; MSEEGPQVKI REASKDNVDF ILSNVDLAMA NSLRRVMIAE IPTLAIDSVE VETNTTVLAD EFIAHRLGLI PLQSMDIEQL EYSRDCFCED HCDKCSVVLT LQAFGESEST TNVYSKDLVI VSNLMGRNIG HPIIQDKEGN GVLICKLRKG QELKLTCVAK KGIAKEHAKW GPAAAIEFEY DPWNKLKHTD YWYEQDSAKE WPQSKNCEYE DPPNEGDPFD YKAQADTFYM NVESVGSIPV DQVVVRGIDT LQKKVASILL ALTQMDQDKV NFASGDNNTA SNMLGSNEDV MMTGAEQDPY SNASQMGNTG SGGYDNAW //