RPB9_YEAST
ID RPB9_YEAST Reviewed; 122 AA.
AC P27999; D6VU72;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB9;
DE Short=RNA polymerase II subunit B9;
DE AltName: Full=B12.6;
DE AltName: Full=DNA-directed RNA polymerase II 14.2 kDa polypeptide;
DE AltName: Full=DNA-directed RNA polymerase II subunit 9;
GN Name=RPB9; OrderedLocusNames=YGL070C;
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 46-62.
RX PubMed=1918023; DOI=10.1016/s0021-9258(18)55171-1;
RA Woychik N.A., Lane W.S., Young R.A.;
RT "Yeast RNA polymerase II subunit RPB9 is essential for growth at
RT temperature extremes.";
RL J. Biol. Chem. 266:19053-19055(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 INVOLVEMENT IN TRANSCRIPTION ELONGATION.
RX PubMed=10938084; DOI=10.1074/jbc.m004721200;
RA Hemming S.A., Jansma D.B., Macgregor P.F., Goryachev A., Friesen J.D.,
RA Edwards A.M.;
RT "RNA polymerase II subunit Rpb9 regulates transcription elongation in
RT vivo.";
RL J. Biol. Chem. 275:35506-35511(2000).
RN [7]
RP FUNCTION IN DNA REPAIR.
RX PubMed=12411509; DOI=10.1093/emboj/cdf589;
RA Li S., Smerdon M.J.;
RT "Rpb4 and Rpb9 mediate subpathways of transcription-coupled DNA repair in
RT Saccharomyces cerevisiae.";
RL EMBO J. 21:5921-5929(2002).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, 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 [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX IN
RP COMPLEX WITH ZINC IONS, AND SUBUNIT.
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 [12]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE RNA POL II CORE COMPLEX IN
RP COMPLEX WITH ZINC IONS, AND SUBUNIT.
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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX IN
RP COMPLEX WITH ALPHA-AMANITIN AND ZINC IONS, AND SUBUNIT.
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 [14]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN COMPLEX
RP WITH DST1, AND SUBUNIT.
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 [15]
RP X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS) OF THE RNA POL II COMPLEX, AND
RP SUBUNIT.
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 [16]
RP X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF THE RNA POL II CORE COMPLEX, AND
RP SUBUNIT.
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 [17]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF THE RNA POL II CORE COMPLEX IN
RP COMPLEX WITH ZINC IONS, AND SUBUNIT.
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 [18]
RP X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS), AND SUBUNIT.
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 [19]
RP X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS) OF THE RNA POL II CORE COMPLEX, AND
RP SUBUNIT.
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 [20]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX, AND
RP SUBUNIT.
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 [21]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN COMPLEX
RP WITH INHIBITING NON-CODING RNA, AND SUBUNIT.
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 [22]
RP X-RAY CRYSTALLOGRAPHY (4.15 ANGSTROMS) OF THE RNA POL II COMPLEX, AND
RP SUBUNIT.
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. RPB9 is part of the
CC upper jaw surrounding the central large cleft and thought to grab the
CC incoming DNA template. Involved in the regulation of transcription
CC elongation. Involved in DNA repair of damage in the transcribed strand.
CC Mediates a transcription-coupled repair (TCR) subpathway of nucleotide
CC excision repair (NER). {ECO:0000269|PubMed:12411509}.
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. {ECO:0000269|PubMed:11313498,
CC ECO:0000269|PubMed:11313499, ECO:0000269|PubMed:11805306,
CC ECO:0000269|PubMed:12746495, ECO:0000269|PubMed:12746498,
CC ECO:0000269|PubMed:12914699, ECO:0000269|PubMed:14963322,
CC ECO:0000269|PubMed:15537538, ECO:0000269|PubMed:15591044,
CC ECO:0000269|PubMed:15610738, ECO:0000269|PubMed:16341226,
CC ECO:0000269|PubMed:16765890}.
CC -!- INTERACTION:
CC P27999; P20436: RPB8; NbExp=3; IntAct=EBI-15798, EBI-15794;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P32529}.
CC -!- MISCELLANEOUS: Present with 2440 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000305}.
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DR EMBL; M73060; AAA34997.1; -; Genomic_DNA.
DR EMBL; Z72592; CAA96774.1; -; Genomic_DNA.
DR EMBL; AY557799; AAS56125.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08033.1; -; Genomic_DNA.
DR PIR; A41016; RNBY29.
DR RefSeq; NP_011445.1; NM_001180935.1.
DR PDB; 1I3Q; X-ray; 3.10 A; I=1-122.
DR PDB; 1I50; X-ray; 2.80 A; I=1-122.
DR PDB; 1I6H; X-ray; 3.30 A; I=1-122.
DR PDB; 1K83; X-ray; 2.80 A; I=1-122.
DR PDB; 1NIK; X-ray; 4.10 A; I=1-122.
DR PDB; 1NT9; X-ray; 4.20 A; I=1-122.
DR PDB; 1PQV; X-ray; 3.80 A; I=1-122.
DR PDB; 1R5U; X-ray; 4.50 A; I=1-122.
DR PDB; 1R9S; X-ray; 4.25 A; I=1-122.
DR PDB; 1R9T; X-ray; 3.50 A; I=1-122.
DR PDB; 1SFO; X-ray; 3.61 A; I=1-122.
DR PDB; 1TWA; X-ray; 3.20 A; I=1-122.
DR PDB; 1TWC; X-ray; 3.00 A; I=1-122.
DR PDB; 1TWF; X-ray; 2.30 A; I=1-122.
DR PDB; 1TWG; X-ray; 3.30 A; I=1-122.
DR PDB; 1TWH; X-ray; 3.40 A; I=1-122.
DR PDB; 1WCM; X-ray; 3.80 A; I=1-122.
DR PDB; 1Y1V; X-ray; 3.80 A; I=1-122.
DR PDB; 1Y1W; X-ray; 4.00 A; I=1-122.
DR PDB; 1Y1Y; X-ray; 4.00 A; I=1-122.
DR PDB; 1Y77; X-ray; 4.50 A; I=1-122.
DR PDB; 2B63; X-ray; 3.80 A; I=1-122.
DR PDB; 2B8K; X-ray; 4.15 A; I=1-122.
DR PDB; 2E2H; X-ray; 3.95 A; I=1-122.
DR PDB; 2E2I; X-ray; 3.41 A; I=1-122.
DR PDB; 2E2J; X-ray; 3.50 A; I=1-122.
DR PDB; 2JA5; X-ray; 3.80 A; I=1-122.
DR PDB; 2JA6; X-ray; 4.00 A; I=1-122.
DR PDB; 2JA7; X-ray; 3.80 A; I/U=1-122.
DR PDB; 2JA8; X-ray; 3.80 A; I=1-122.
DR PDB; 2NVQ; X-ray; 2.90 A; I=1-122.
DR PDB; 2NVT; X-ray; 3.36 A; I=1-122.
DR PDB; 2NVX; X-ray; 3.60 A; I=1-122.
DR PDB; 2NVY; X-ray; 3.40 A; I=1-122.
DR PDB; 2NVZ; X-ray; 4.30 A; I=1-122.
DR PDB; 2R7Z; X-ray; 3.80 A; I=1-122.
DR PDB; 2R92; X-ray; 3.80 A; I=1-122.
DR PDB; 2R93; X-ray; 4.00 A; I=1-122.
DR PDB; 2VUM; X-ray; 3.40 A; I=1-122.
DR PDB; 2YU9; X-ray; 3.40 A; I=1-122.
DR PDB; 3CQZ; X-ray; 2.80 A; I=1-122.
DR PDB; 3FKI; X-ray; 3.88 A; I=1-122.
DR PDB; 3GTG; X-ray; 3.78 A; I=1-122.
DR PDB; 3GTJ; X-ray; 3.42 A; I=1-122.
DR PDB; 3GTK; X-ray; 3.80 A; I=1-122.
DR PDB; 3GTL; X-ray; 3.38 A; I=1-122.
DR PDB; 3GTM; X-ray; 3.80 A; I=1-122.
DR PDB; 3GTO; X-ray; 4.00 A; I=1-122.
DR PDB; 3GTP; X-ray; 3.90 A; I=1-122.
DR PDB; 3GTQ; X-ray; 3.80 A; I=1-122.
DR PDB; 3H3V; X-ray; 4.00 A; J=1-122.
DR PDB; 3HOU; X-ray; 3.20 A; I/U=1-122.
DR PDB; 3HOV; X-ray; 3.50 A; I=1-122.
DR PDB; 3HOW; X-ray; 3.60 A; I=1-122.
DR PDB; 3HOX; X-ray; 3.65 A; I=1-122.
DR PDB; 3HOY; X-ray; 3.40 A; I=1-122.
DR PDB; 3HOZ; X-ray; 3.65 A; I=1-122.
DR PDB; 3I4M; X-ray; 3.70 A; I=1-122.
DR PDB; 3I4N; X-ray; 3.90 A; I=1-122.
DR PDB; 3J0K; EM; 36.00 A; I=1-122.
DR PDB; 3J1N; EM; 16.00 A; I=1-122.
DR PDB; 3K1F; X-ray; 4.30 A; I=1-122.
DR PDB; 3K7A; X-ray; 3.80 A; I=1-122.
DR PDB; 3M3Y; X-ray; 3.18 A; I=1-122.
DR PDB; 3M4O; X-ray; 3.57 A; I=1-122.
DR PDB; 3PO2; X-ray; 3.30 A; I=1-122.
DR PDB; 3PO3; X-ray; 3.30 A; I=1-122.
DR PDB; 3QT1; X-ray; 4.30 A; I=1-87.
DR PDB; 3RZD; X-ray; 3.30 A; I=1-122.
DR PDB; 3RZO; X-ray; 3.00 A; I=1-122.
DR PDB; 3S14; X-ray; 2.85 A; I=1-122.
DR PDB; 3S15; X-ray; 3.30 A; I=1-122.
DR PDB; 3S16; X-ray; 3.24 A; I=1-122.
DR PDB; 3S17; X-ray; 3.20 A; I=1-122.
DR PDB; 3S1M; X-ray; 3.13 A; I=1-122.
DR PDB; 3S1N; X-ray; 3.10 A; I=1-122.
DR PDB; 3S1Q; X-ray; 3.30 A; I=1-122.
DR PDB; 3S1R; X-ray; 3.20 A; I=1-122.
DR PDB; 3S2D; X-ray; 3.20 A; I=1-122.
DR PDB; 3S2H; X-ray; 3.30 A; I=1-122.
DR PDB; 4A3B; X-ray; 3.50 A; I=1-122.
DR PDB; 4A3C; X-ray; 3.50 A; I=1-122.
DR PDB; 4A3D; X-ray; 3.40 A; I=1-122.
DR PDB; 4A3E; X-ray; 3.40 A; I=1-122.
DR PDB; 4A3F; X-ray; 3.50 A; I=1-122.
DR PDB; 4A3G; X-ray; 3.50 A; I=1-122.
DR PDB; 4A3I; X-ray; 3.80 A; I=1-122.
DR PDB; 4A3J; X-ray; 3.70 A; I=1-122.
DR PDB; 4A3K; X-ray; 3.50 A; I=1-122.
DR PDB; 4A3L; X-ray; 3.50 A; I=1-122.
DR PDB; 4A3M; X-ray; 3.90 A; I=1-122.
DR PDB; 4A93; X-ray; 3.40 A; I=1-122.
DR PDB; 4BBR; X-ray; 3.40 A; I=1-122.
DR PDB; 4BBS; X-ray; 3.60 A; I=1-122.
DR PDB; 4BXX; X-ray; 3.28 A; I=1-122.
DR PDB; 4BXZ; X-ray; 4.80 A; I=1-122.
DR PDB; 4BY1; X-ray; 3.60 A; I=1-122.
DR PDB; 4BY7; X-ray; 3.15 A; I=1-122.
DR PDB; 4V1M; EM; 6.60 A; I=1-122.
DR PDB; 4V1N; EM; 7.80 A; I=1-122.
DR PDB; 4V1O; EM; 9.70 A; I=1-122.
DR PDB; 4X67; X-ray; 4.10 A; I=1-122.
DR PDB; 4X6A; X-ray; 3.96 A; I=1-122.
DR PDB; 4Y52; X-ray; 3.50 A; I=1-122.
DR PDB; 4Y7N; X-ray; 3.30 A; I=1-122.
DR PDB; 5C3E; X-ray; 3.70 A; I=1-122.
DR PDB; 5C44; X-ray; 3.95 A; I=1-120.
DR PDB; 5C4A; X-ray; 4.20 A; I=1-122.
DR PDB; 5C4J; X-ray; 4.00 A; I=1-122.
DR PDB; 5C4X; X-ray; 4.00 A; I=1-122.
DR PDB; 5FMF; EM; 6.00 A; I=2-120.
DR PDB; 5FYW; EM; 4.35 A; I=1-122.
DR PDB; 5FZ5; EM; 8.80 A; I=1-122.
DR PDB; 5IP7; X-ray; 3.52 A; I=2-120.
DR PDB; 5IP9; X-ray; 3.90 A; I=2-120.
DR PDB; 5OQJ; EM; 4.70 A; I=1-122.
DR PDB; 5OQM; EM; 5.80 A; I=1-122.
DR PDB; 5OT2; X-ray; 3.20 A; I=1-122.
DR PDB; 5SVA; EM; 15.30 A; I=1-122.
DR PDB; 5U5Q; X-ray; 3.80 A; I=1-122.
DR PDB; 5VVR; EM; 5.80 A; I=1-122.
DR PDB; 5VVS; EM; 6.40 A; I=1-122.
DR PDB; 5W4U; X-ray; 3.60 A; I=1-122.
DR PDB; 5W51; X-ray; 3.40 A; I=1-122.
DR PDB; 6BLO; X-ray; 3.40 A; I=1-122.
DR PDB; 6BLP; X-ray; 3.20 A; I=1-122.
DR PDB; 6BM2; X-ray; 3.40 A; I=1-122.
DR PDB; 6BM4; X-ray; 2.95 A; I=1-122.
DR PDB; 6BQF; X-ray; 3.35 A; I=1-122.
DR PDB; 6GYK; EM; 5.10 A; I=1-122.
DR PDB; 6GYL; EM; 4.80 A; I=1-122.
DR PDB; 6GYM; EM; 6.70 A; I=1-122.
DR PDB; 6I84; EM; 4.40 A; I=1-122.
DR PDB; 6O6C; EM; 3.10 A; G=1-122.
DR PDB; 6UPX; X-ray; 3.40 A; I=1-122.
DR PDB; 6UPY; X-ray; 3.40 A; I=1-122.
DR PDB; 6UPZ; X-ray; 3.10 A; I=1-122.
DR PDB; 6UQ0; X-ray; 3.56 A; I=1-122.
DR PDB; 6UQ1; X-ray; 3.60 A; I=1-122.
DR PDB; 6UQ2; X-ray; 3.20 A; I=1-122.
DR PDB; 6UQ3; X-ray; 3.47 A; I=1-122.
DR PDB; 7KED; X-ray; 3.60 A; I=1-122.
DR PDB; 7KEE; X-ray; 3.45 A; I=1-122.
DR PDB; 7KEF; X-ray; 3.89 A; I=1-122.
DR PDB; 7NKX; EM; 2.90 A; I=1-122.
DR PDB; 7NKY; EM; 3.20 A; I=1-122.
DR PDB; 7O4I; EM; 3.20 A; I=1-122.
DR PDB; 7O4J; EM; 2.90 A; I=1-122.
DR PDB; 7O72; EM; 3.40 A; I=1-122.
DR PDB; 7O73; EM; 3.40 A; I=1-122.
DR PDB; 7O75; EM; 3.20 A; I=1-122.
DR PDB; 7RIM; X-ray; 2.90 A; I=1-122.
DR PDB; 7RIP; X-ray; 3.30 A; I=1-122.
DR PDB; 7RIQ; X-ray; 3.00 A; I=1-122.
DR PDB; 7RIW; X-ray; 3.20 A; I=1-122.
DR PDB; 7RIX; X-ray; 3.40 A; I=1-122.
DR PDB; 7RIY; X-ray; 3.70 A; I=1-122.
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; P27999; -.
DR SMR; P27999; -.
DR BioGRID; 33178; 94.
DR ComplexPortal; CPX-2662; DNA-directed RNA polymerase II complex.
DR DIP; DIP-610N; -.
DR IntAct; P27999; 21.
DR MINT; P27999; -.
DR STRING; 4932.YGL070C; -.
DR iPTMnet; P27999; -.
DR PaxDb; P27999; -.
DR PRIDE; P27999; -.
DR EnsemblFungi; YGL070C_mRNA; YGL070C; YGL070C.
DR GeneID; 852810; -.
DR KEGG; sce:YGL070C; -.
DR SGD; S000003038; RPB9.
DR VEuPathDB; FungiDB:YGL070C; -.
DR eggNOG; KOG2691; Eukaryota.
DR GeneTree; ENSGT00550000075063; -.
DR HOGENOM; CLU_093932_0_1_1; -.
DR InParanoid; P27999; -.
DR OMA; CRDCNNM; -.
DR BioCyc; YEAST:G3O-30573-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; P27999; -.
DR PRO; PR:P27999; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P27999; protein.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:SGD.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001193; P:maintenance of transcriptional fidelity during DNA-templated transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006379; P:mRNA cleavage; IEA:InterPro.
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 GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IGI:SGD.
DR CDD; cd10508; Zn-ribbon_RPB9; 1.
DR InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS.
DR InterPro; IPR034012; Zn_ribbon_RPB9_C.
DR InterPro; IPR001222; Znf_TFIIS.
DR PANTHER; PTHR11239; PTHR11239; 1.
DR Pfam; PF02150; RNA_POL_M_15KD; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR PIRSF; PIRSF005586; RNApol_RpoM; 1.
DR SMART; SM00661; RPOL9; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA repair;
KW DNA-directed RNA polymerase; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Zinc; Zinc-finger.
FT CHAIN 1..122
FT /note="DNA-directed RNA polymerase II subunit RPB9"
FT /id="PRO_0000121474"
FT ZN_FING 7..32
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 71..111
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11313498,
FT ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538,
FT ECO:0000305|PubMed:11313499"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11313498,
FT ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538,
FT ECO:0000305|PubMed:11313499"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11313498,
FT ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538,
FT ECO:0000305|PubMed:11313499"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11313498,
FT ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538,
FT ECO:0000305|PubMed:11313499"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306,
FT ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306,
FT ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306,
FT ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472,
FT ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306,
FT ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 52..57
FT /evidence="ECO:0007829|PDB:1I50"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3S1N"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:7NKX"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:3S16"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:2NVQ"
SQ SEQUENCE 122 AA; 14288 MW; A80D69678A722881 CRC64;
MTTFRFCRDC NNMLYPREDK ENNRLLFECR TCSYVEEAGS PLVYRHELIT NIGETAGVVQ
DIGSDPTLPR SDRECPKCHS RENVFFQSQQ RRKDTSMVLF FVCLSCSHIF TSDQKNKRTQ
FS
