RPB3_YEAST
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 03-AUG-2022, entry version 216.
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}.
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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; 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 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; 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 AlphaFoldDB; P16370; -.
DR SMR; P16370; -.
DR BioGRID; 34967; 891.
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; P16370; -.
DR PRIDE; P16370; -.
DR EnsemblFungi; YIL021W_mRNA; YIL021W; YIL021W.
DR GeneID; 854791; -.
DR KEGG; sce:YIL021W; -.
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 BioCyc; YEAST:G3O-31296-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-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-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
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; IC: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: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 from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0001172; P:transcription, RNA-templated; IEA:GOC.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 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 Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 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
