RPB11_YEAST
ID RPB11_YEAST Reviewed; 120 AA.
AC P38902; D6W262;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB11;
DE Short=RNA polymerase II subunit B11;
DE AltName: Full=B13.6;
DE AltName: Full=DNA-directed RNA polymerase II 13.6 kDa polypeptide;
GN Name=RPB11; OrderedLocusNames=YOL005C;
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 27-37; 75-84;
RP 98-102 AND 103-116.
RC STRAIN=X2180-2;
RX PubMed=8508029;
RA Woychik N.A., McKune K., Lane W.S., Young R.A.;
RT "Yeast RNA polymerase II subunit RPB11 is related to a subunit shared by
RT RNA polymerase I and III.";
RL Gene Expr. 3:77-82(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
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 [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 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 [5]
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 [6]
RP FUNCTION, AND MUTAGENESIS OF GLU-108; LEU-111 AND LEU-114.
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 [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. RPB11 is part of the
CC core element with the central large cleft. Seems to be involved
CC transcript 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 P38902; P16370: RPB3; NbExp=4; IntAct=EBI-15806, EBI-15773;
CC P38902; P20436: RPB8; NbExp=3; IntAct=EBI-15806, EBI-15794;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA
CC polymerase subunit family. {ECO:0000305}.
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DR EMBL; S62624; AAB27135.1; -; Genomic_DNA.
DR EMBL; Z74747; CAA99004.1; -; Genomic_DNA.
DR EMBL; AY557998; AAS56324.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10778.1; -; Genomic_DNA.
DR PIR; S58933; S58933.
DR RefSeq; NP_014638.1; NM_001183259.1.
DR PDB; 1I3Q; X-ray; 3.10 A; K=1-120.
DR PDB; 1I50; X-ray; 2.80 A; K=1-120.
DR PDB; 1I6H; X-ray; 3.30 A; K=1-120.
DR PDB; 1K83; X-ray; 2.80 A; K=1-120.
DR PDB; 1NIK; X-ray; 4.10 A; K=1-120.
DR PDB; 1NT9; X-ray; 4.20 A; K=1-120.
DR PDB; 1PQV; X-ray; 3.80 A; K=1-120.
DR PDB; 1R5U; X-ray; 4.50 A; K=1-120.
DR PDB; 1R9S; X-ray; 4.25 A; K=1-120.
DR PDB; 1R9T; X-ray; 3.50 A; K=1-120.
DR PDB; 1SFO; X-ray; 3.61 A; K=1-120.
DR PDB; 1TWA; X-ray; 3.20 A; K=1-120.
DR PDB; 1TWC; X-ray; 3.00 A; K=1-120.
DR PDB; 1TWF; X-ray; 2.30 A; K=1-120.
DR PDB; 1TWG; X-ray; 3.30 A; K=1-120.
DR PDB; 1TWH; X-ray; 3.40 A; K=1-120.
DR PDB; 1WCM; X-ray; 3.80 A; K=1-120.
DR PDB; 1Y1V; X-ray; 3.80 A; K=1-120.
DR PDB; 1Y1W; X-ray; 4.00 A; K=1-120.
DR PDB; 1Y1Y; X-ray; 4.00 A; K=1-120.
DR PDB; 1Y77; X-ray; 4.50 A; K=1-120.
DR PDB; 2B63; X-ray; 3.80 A; K=1-120.
DR PDB; 2B8K; X-ray; 4.15 A; K=1-120.
DR PDB; 2E2H; X-ray; 3.95 A; K=1-120.
DR PDB; 2E2I; X-ray; 3.41 A; K=1-120.
DR PDB; 2E2J; X-ray; 3.50 A; K=1-120.
DR PDB; 2JA5; X-ray; 3.80 A; K=1-120.
DR PDB; 2JA6; X-ray; 4.00 A; K=1-120.
DR PDB; 2JA7; X-ray; 3.80 A; K/W=1-120.
DR PDB; 2JA8; X-ray; 3.80 A; K=1-120.
DR PDB; 2NVQ; X-ray; 2.90 A; K=1-120.
DR PDB; 2NVT; X-ray; 3.36 A; K=1-120.
DR PDB; 2NVX; X-ray; 3.60 A; K=1-120.
DR PDB; 2NVY; X-ray; 3.40 A; K=1-120.
DR PDB; 2NVZ; X-ray; 4.30 A; K=1-120.
DR PDB; 2R7Z; X-ray; 3.80 A; K=1-120.
DR PDB; 2R92; X-ray; 3.80 A; K=1-120.
DR PDB; 2R93; X-ray; 4.00 A; K=1-120.
DR PDB; 2VUM; X-ray; 3.40 A; K=1-120.
DR PDB; 2YU9; X-ray; 3.40 A; K=1-120.
DR PDB; 3CQZ; X-ray; 2.80 A; K=1-120.
DR PDB; 3FKI; X-ray; 3.88 A; K=1-120.
DR PDB; 3GTG; X-ray; 3.78 A; K=1-120.
DR PDB; 3GTJ; X-ray; 3.42 A; K=1-120.
DR PDB; 3GTK; X-ray; 3.80 A; K=1-120.
DR PDB; 3GTL; X-ray; 3.38 A; K=1-120.
DR PDB; 3GTM; X-ray; 3.80 A; K=1-120.
DR PDB; 3GTO; X-ray; 4.00 A; K=1-120.
DR PDB; 3GTP; X-ray; 3.90 A; K=1-120.
DR PDB; 3GTQ; X-ray; 3.80 A; K=1-120.
DR PDB; 3H3V; X-ray; 4.00 A; L=1-120.
DR PDB; 3HOU; X-ray; 3.20 A; K/W=1-120.
DR PDB; 3HOV; X-ray; 3.50 A; K=1-120.
DR PDB; 3HOW; X-ray; 3.60 A; K=1-120.
DR PDB; 3HOX; X-ray; 3.65 A; K=1-120.
DR PDB; 3HOY; X-ray; 3.40 A; K=1-120.
DR PDB; 3HOZ; X-ray; 3.65 A; K=1-120.
DR PDB; 3I4M; X-ray; 3.70 A; K=1-120.
DR PDB; 3I4N; X-ray; 3.90 A; K=1-120.
DR PDB; 3J0K; EM; 36.00 A; K=1-120.
DR PDB; 3J1N; EM; 16.00 A; K=1-120.
DR PDB; 3K1F; X-ray; 4.30 A; K=1-120.
DR PDB; 3K7A; X-ray; 3.80 A; K=1-120.
DR PDB; 3M3Y; X-ray; 3.18 A; K=1-120.
DR PDB; 3M4O; X-ray; 3.57 A; K=1-120.
DR PDB; 3PO2; X-ray; 3.30 A; K=1-120.
DR PDB; 3PO3; X-ray; 3.30 A; K=1-120.
DR PDB; 3QT1; X-ray; 4.30 A; K=1-120.
DR PDB; 3RZD; X-ray; 3.30 A; K=1-120.
DR PDB; 3RZO; X-ray; 3.00 A; K=1-120.
DR PDB; 3S14; X-ray; 2.85 A; K=1-120.
DR PDB; 3S15; X-ray; 3.30 A; K=1-120.
DR PDB; 3S16; X-ray; 3.24 A; K=1-120.
DR PDB; 3S17; X-ray; 3.20 A; K=1-120.
DR PDB; 3S1M; X-ray; 3.13 A; K=1-120.
DR PDB; 3S1N; X-ray; 3.10 A; K=1-120.
DR PDB; 3S1Q; X-ray; 3.30 A; K=1-120.
DR PDB; 3S1R; X-ray; 3.20 A; K=1-120.
DR PDB; 3S2D; X-ray; 3.20 A; K=1-120.
DR PDB; 3S2H; X-ray; 3.30 A; K=1-120.
DR PDB; 4A3B; X-ray; 3.50 A; K=1-120.
DR PDB; 4A3C; X-ray; 3.50 A; K=1-120.
DR PDB; 4A3D; X-ray; 3.40 A; K=1-120.
DR PDB; 4A3E; X-ray; 3.40 A; K=1-120.
DR PDB; 4A3F; X-ray; 3.50 A; K=1-120.
DR PDB; 4A3G; X-ray; 3.50 A; K=1-120.
DR PDB; 4A3I; X-ray; 3.80 A; K=1-120.
DR PDB; 4A3J; X-ray; 3.70 A; K=1-120.
DR PDB; 4A3K; X-ray; 3.50 A; K=1-120.
DR PDB; 4A3L; X-ray; 3.50 A; K=1-120.
DR PDB; 4A3M; X-ray; 3.90 A; K=1-120.
DR PDB; 4A93; X-ray; 3.40 A; K=1-120.
DR PDB; 4BBR; X-ray; 3.40 A; K=1-120.
DR PDB; 4BBS; X-ray; 3.60 A; K=1-120.
DR PDB; 4BXX; X-ray; 3.28 A; K=1-120.
DR PDB; 4BXZ; X-ray; 4.80 A; K=1-120.
DR PDB; 4BY1; X-ray; 3.60 A; K=1-120.
DR PDB; 4BY7; X-ray; 3.15 A; K=1-120.
DR PDB; 4V1M; EM; 6.60 A; K=1-120.
DR PDB; 4V1N; EM; 7.80 A; K=1-120.
DR PDB; 4V1O; EM; 9.70 A; K=1-120.
DR PDB; 4X67; X-ray; 4.10 A; K=1-120.
DR PDB; 4X6A; X-ray; 3.96 A; K=1-120.
DR PDB; 4Y52; X-ray; 3.50 A; K=1-120.
DR PDB; 4Y7N; X-ray; 3.30 A; K=1-120.
DR PDB; 5C3E; X-ray; 3.70 A; K=1-120.
DR PDB; 5C44; X-ray; 3.95 A; K=1-120.
DR PDB; 5C4A; X-ray; 4.20 A; K=1-120.
DR PDB; 5C4J; X-ray; 4.00 A; K=1-120.
DR PDB; 5C4X; X-ray; 4.00 A; K=1-120.
DR PDB; 5FMF; EM; 6.00 A; K=1-115.
DR PDB; 5FYW; EM; 4.35 A; K=1-120.
DR PDB; 5FZ5; EM; 8.80 A; K=1-120.
DR PDB; 5IP7; X-ray; 3.52 A; K=1-115.
DR PDB; 5IP9; X-ray; 3.90 A; K=1-115.
DR PDB; 5OQJ; EM; 4.70 A; K=1-120.
DR PDB; 5OQM; EM; 5.80 A; K=1-120.
DR PDB; 5OT2; X-ray; 3.20 A; K=1-120.
DR PDB; 5SVA; EM; 15.30 A; K=1-120.
DR PDB; 5U5Q; X-ray; 3.80 A; K=1-120.
DR PDB; 5VVR; EM; 5.80 A; K=1-120.
DR PDB; 5VVS; EM; 6.40 A; K=1-120.
DR PDB; 5W4U; X-ray; 3.60 A; K=1-120.
DR PDB; 5W51; X-ray; 3.40 A; K=1-120.
DR PDB; 6BLO; X-ray; 3.40 A; K=1-120.
DR PDB; 6BLP; X-ray; 3.20 A; K=1-120.
DR PDB; 6BM2; X-ray; 3.40 A; K=1-120.
DR PDB; 6BM4; X-ray; 2.95 A; K=1-120.
DR PDB; 6BQF; X-ray; 3.35 A; K=1-120.
DR PDB; 6GYK; EM; 5.10 A; K=1-120.
DR PDB; 6GYL; EM; 4.80 A; K=1-120.
DR PDB; 6GYM; EM; 6.70 A; K=1-120.
DR PDB; 6I84; EM; 4.40 A; K=1-120.
DR PDB; 6O6C; EM; 3.10 A; I=1-120.
DR PDB; 6UPX; X-ray; 3.40 A; K=1-120.
DR PDB; 6UPY; X-ray; 3.40 A; K=1-120.
DR PDB; 6UPZ; X-ray; 3.10 A; K=1-120.
DR PDB; 6UQ0; X-ray; 3.56 A; K=1-120.
DR PDB; 6UQ1; X-ray; 3.60 A; K=1-120.
DR PDB; 6UQ2; X-ray; 3.20 A; K=1-120.
DR PDB; 6UQ3; X-ray; 3.47 A; K=1-120.
DR PDB; 7KED; X-ray; 3.60 A; K=1-120.
DR PDB; 7KEE; X-ray; 3.45 A; K=1-120.
DR PDB; 7KEF; X-ray; 3.89 A; K=1-120.
DR PDB; 7NKX; EM; 2.90 A; K=1-120.
DR PDB; 7NKY; EM; 3.20 A; K=1-120.
DR PDB; 7O4I; EM; 3.20 A; K=1-120.
DR PDB; 7O4J; EM; 2.90 A; K=1-120.
DR PDB; 7O72; EM; 3.40 A; K=1-120.
DR PDB; 7O73; EM; 3.40 A; K=1-120.
DR PDB; 7O75; EM; 3.20 A; K=1-120.
DR PDB; 7RIM; X-ray; 2.90 A; K=1-120.
DR PDB; 7RIP; X-ray; 3.30 A; K=1-120.
DR PDB; 7RIQ; X-ray; 3.00 A; K=1-120.
DR PDB; 7RIW; X-ray; 3.20 A; K=1-120.
DR PDB; 7RIX; X-ray; 3.40 A; K=1-120.
DR PDB; 7RIY; X-ray; 3.70 A; K=1-120.
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; P38902; -.
DR SMR; P38902; -.
DR BioGRID; 34399; 393.
DR ComplexPortal; CPX-2662; DNA-directed RNA polymerase II complex.
DR DIP; DIP-937N; -.
DR IntAct; P38902; 21.
DR MINT; P38902; -.
DR STRING; 4932.YOL005C; -.
DR iPTMnet; P38902; -.
DR MaxQB; P38902; -.
DR PaxDb; P38902; -.
DR PRIDE; P38902; -.
DR EnsemblFungi; YOL005C_mRNA; YOL005C; YOL005C.
DR GeneID; 854157; -.
DR KEGG; sce:YOL005C; -.
DR SGD; S000005365; RPB11.
DR VEuPathDB; FungiDB:YOL005C; -.
DR eggNOG; KOG4392; Eukaryota.
DR HOGENOM; CLU_090381_2_1_1; -.
DR InParanoid; P38902; -.
DR OMA; LEQACTK; -.
DR BioCyc; YEAST:G3O-33422-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; P38902; -.
DR PRO; PR:P38902; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P38902; protein.
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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0001055; F:RNA polymerase II 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 CDD; cd06926; RNAP_II_RPB11; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00261; RNApol_arch_Rpo11; 1.
DR InterPro; IPR037685; RBP11.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR009025; RBP11-like_dimer.
DR InterPro; IPR008193; RNA_pol_Rpb11_13-16kDa_CS.
DR Pfam; PF13656; RNA_pol_L_2; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR PROSITE; PS01154; RNA_POL_L_13KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-directed RNA polymerase;
KW Nucleus; Reference proteome; Transcription.
FT CHAIN 1..120
FT /note="DNA-directed RNA polymerase II subunit RPB11"
FT /id="PRO_0000149315"
FT MUTAGEN 108
FT /note="E->G,V: Transcript termination readthrough."
FT /evidence="ECO:0000269|PubMed:16537912"
FT MUTAGEN 108
FT /note="E->K: Transcript termination readthrough. Lethal."
FT /evidence="ECO:0000269|PubMed:16537912"
FT MUTAGEN 111
FT /note="L->P: Transcript termination readthrough."
FT /evidence="ECO:0000269|PubMed:16537912"
FT MUTAGEN 114
FT /note="L->P: Transcript termination readthrough."
FT /evidence="ECO:0000269|PubMed:16537912"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:3S2H"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2VUM"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3CQZ"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 83..108
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1TWF"
SQ SEQUENCE 120 AA; 13616 MW; A98D109C5FF8E356 CRC64;
MNAPDRFELF LLGEGESKLK IDPDTKAPNA VVITFEKEDH TLGNLIRAEL LNDRKVLFAA
YKVEHPFFAR FKLRIQTTEG YDPKDALKNA CNSIINKLGA LKTNFETEWN LQTLAADDAF
