(data stored in SCRATCH zone)

SWISSPROT: RPB1_YEAST

ID   RPB1_YEAST              Reviewed;        1733 AA.
AC   P04050; D6VRK8; Q12364; Q92315;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   30-AUG-2017, entry version 200.
DE   RecName: Full=DNA-directed RNA polymerase II subunit RPB1;
DE            Short=RNA polymerase II subunit 1;
DE            Short=RNA polymerase II subunit B1;
DE            EC=2.7.7.6;
DE   AltName: Full=DNA-directed RNA polymerase III largest subunit;
DE   AltName: Full=RNA polymerase II subunit B220;
GN   Name=RPO21; Synonyms=RPB1, RPB220, SUA8; OrderedLocusNames=YDL140C;
GN   ORFNames=D2150;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204626 / S288c / A364A;
RX   PubMed=3896517; DOI=10.1016/0092-8674(85)90117-5;
RA   Allison L.A., Moyle M., Shales M., Ingles C.J.;
RT   "Extensive homology among the largest subunits of eukaryotic and
RT   prokaryotic RNA polymerases.";
RL   Cell 42:599-610(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8972577;
RX   DOI=10.1002/(SICI)1097-0061(199612)12:15<1549::AID-YEA42>3.0.CO;2-S;
RA   Woelfl S., Haneman V., Saluz H.P.;
RT   "Analysis of a 26,756 bp segment from the left arm of yeast chromosome
RT   IV.";
RL   Yeast 12:1549-1554(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1669-1733.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7649444; DOI=10.1111/j.1574-6968.1995.tb07724.x;
RA   Cronan J.E. Jr., Wallace J.C.;
RT   "The gene encoding the biotin-apoprotein ligase of Saccharomyces
RT   cerevisiae.";
RL   FEMS Microbiol. Lett. 130:221-230(1995).
RN   [6]
RP   MUTAGENESIS OF THE CTD.
RX   PubMed=7498765;
RA   West M.L., Corden J.L.;
RT   "Construction and analysis of yeast RNA polymerase II CTD deletion and
RT   substitution mutations.";
RL   Genetics 140:1223-1233(1995).
RN   [7]
RP   PHOSPHORYLATION BY THE TFIIK COMPLEX AND THE SRB8-11 COMPLEX.
RX   PubMed=9702190; DOI=10.1016/S1097-2765(00)80112-4;
RA   Hengartner C.J., Myer V.E., Liao S.-M., Wilson C.J., Koh S.S.,
RA   Young R.A.;
RT   "Temporal regulation of RNA polymerase II by Srb10 and Kin28 cyclin-
RT   dependent kinases.";
RL   Mol. Cell 2:43-53(1998).
RN   [8]
RP   INTERACTION WITH ESS1.
RX   PubMed=10531363; DOI=10.1074/jbc.274.44.31583;
RA   Morris D.P., Phatnani H.P., Greenleaf A.L.;
RT   "Phospho-carboxyl-terminal domain binding and the role of a prolyl
RT   isomerase in pre-mRNA 3'-End formation.";
RL   J. Biol. Chem. 274:31583-31587(1999).
RN   [9]
RP   DEPHOSPHORYLATION BY FCP1.
RX   PubMed=10445027; DOI=10.1016/S1097-2765(00)80187-2;
RA   Kobor M.S., Archambault J., Lester W., Holstege F.C.P., Gileadi O.,
RA   Jansma D.B., Jennings E.G., Kouyoumdjian F., Davidson A.R.,
RA   Young R.A., Greenblatt J.;
RT   "An unusual eukaryotic protein phosphatase required for transcription
RT   by RNA polymerase II and CTD dephosphorylation in S. cerevisiae.";
RL   Mol. Cell 4:55-62(1999).
RN   [10]
RP   PHOSPHORYLATION BY THE BUR KINASE COMPLEX.
RX   PubMed=11390638; DOI=10.1128/MCB.21.13.4089-4096.2001;
RA   Murray S., Udupa R., Yao S., Hartzog G., Prelich G.;
RT   "Phosphorylation of the RNA polymerase II carboxy-terminal domain by
RT   the Bur1 cyclin-dependent kinase.";
RL   Mol. Cell. Biol. 21:4089-4096(2001).
RN   [11]
RP   INTERACTION WITH ASK10.
RX   PubMed=14555478; DOI=10.1128/EC.2.5.962-970.2003;
RA   Cohen T.J., Lee K., Rutkowski L.H., Strich R.;
RT   "Ask10p mediates the oxidative stress-induced destruction of the
RT   Saccharomyces cerevisiae C-type cyclin Ume3p/Srb11p.";
RL   Eukaryot. Cell 2:962-970(2003).
RN   [12]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-695, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RX   PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA   Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT   "A subset of membrane-associated proteins is ubiquitinated in response
RT   to mutations in the endoplasmic reticulum degradation machinery.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN   [13]
RP   PHOSPHORYLATION BY CTD KINASE.
RX   PubMed=15047695; DOI=10.1074/jbc.M402218200;
RA   Jones J.C., Phatnani H.P., Haystead T.A., MacDonald J.A., Alam S.M.,
RA   Greenleaf A.L.;
RT   "C-terminal repeat domain kinase I phosphorylates Ser2 and Ser5 of RNA
RT   polymerase II C-terminal domain repeats.";
RL   J. Biol. Chem. 279:24957-24964(2004).
RN   [14]
RP   INTERACTION WITH RTT103.
RX   PubMed=15565157; DOI=10.1038/nature03041;
RA   Kim M., Krogan N.J., Vasiljeva L., Rando O.J., Nedea E.,
RA   Greenblatt J.F., Buratowski S.;
RT   "The yeast Rat1 exonuclease promotes transcription termination by RNA
RT   polymerase II.";
RL   Nature 432:517-522(2004).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1471, AND IDENTIFICATION
RP   BY 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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [17]
RP   INTERACTION WITH SHE2.
RX   PubMed=20713510; DOI=10.1101/gad.1937510;
RA   Shen Z., St-Denis A., Chartrand P.;
RT   "Cotranscriptional recruitment of She2p by RNA pol II elongation
RT   factor Spt4-Spt5/DSIF promotes mRNA localization to the yeast bud.";
RL   Genes Dev. 24:1914-1926(2010).
RN   [18]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-695; LYS-1246 AND
RP   LYS-1350, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
RN   [19]
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.,
RA   Bareket-Samish A., 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   [20]
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   [21]
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
RT   complex at 3.3 A resolution.";
RL   Science 292:1876-1882(2001).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE RNA POL II CORE COMPLEX
RP   IN 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   [23]
RP   X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN
RP   COMPLEX WITH DST1.
RX   PubMed=12914699; DOI=10.1016/S0092-8674(03)00598-1;
RA   Kettenberger H., Armache K.J., Cramer P.;
RT   "Architecture of the RNA polymerase II-TFIIS complex and implications
RT   for mRNA cleavage.";
RL   Cell 114:347-357(2003).
RN   [24]
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   [25]
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:
RT   implications for the initiation of transcription.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:6969-6973(2003).
RN   [26]
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
RT   in the RNA polymerase II active center.";
RL   Cell 119:481-489(2004).
RN   [27]
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   [28]
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
RT   cocrystal at 4.5 Angstroms.";
RL   Science 303:983-988(2004).
RN   [29]
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,
RT   Rpb4/7.";
RL   J. Biol. Chem. 280:7131-7134(2005).
RN   [30]
RP   X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF THE RNA POL II COMPLEX IN
RP   COMPLEX 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   [31]
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
RT   updated structural model.";
RL   Structure 14:973-982(2006).
RN   [32]
RP   X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP   ZINC.
RX   PubMed=23151482; DOI=10.1038/nature11715;
RA   Sainsbury S., Niesser J., Cramer P.;
RT   "Structure and function of the initially transcribing RNA polymerase
RT   II-TFIIB complex.";
RL   Nature 493:437-440(2013).
RN   [33]
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.60 ANGSTROMS) IN COMPLEX WITH
RP   MAGNESIUM AND ZINC.
RX   PubMed=25652824; DOI=10.1038/nature14229;
RA   Plaschka C., Lariviere L., Wenzeck L., Seizl M., Hemann M.,
RA   Tegunov D., Petrotchenko E.V., Borchers C.H., Baumeister W.,
RA   Herzog F., Villa E., Cramer P.;
RT   "Architecture of the RNA polymerase II-Mediator core initiation
RT   complex.";
RL   Nature 518:376-380(2015).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. Largest and catalytic component of RNA polymerase II
CC       which synthesizes mRNA precursors and many functional non-coding
CC       RNAs. Forms the polymerase active center together with the second
CC       largest subunit. Pol II is the central component of the basal RNA
CC       polymerase II transcription machinery. During a transcription
CC       cycle, Pol II, general transcription factors and the Mediator
CC       complex assemble as the preinitiation complex (PIC) at the
CC       promoter. 11-15 base pairs of DNA surrounding the transcription
CC       start site are melted and the single-stranded DNA template strand
CC       of the promoter is positioned deeply within the central active
CC       site cleft of Pol II to form the open complex. After synthesis of
CC       about 30 bases of RNA, Pol II releases its contacts with the core
CC       promoter and the rest of the transcription machinery (promoter
CC       clearance) and enters the stage of transcription elongation in
CC       which it moves on the template as the transcript elongates. Pol II
CC       appears to oscillate between inactive and active conformations at
CC       each step of nucleotide addition. Elongation is influenced by the
CC       phosphorylation status of the C-terminal domain (CTD) of Pol II
CC       largest subunit (RPB1), which serves as a platform for assembly of
CC       factors that regulate transcription initiation, elongation,
CC       termination and mRNA processing. Pol II is composed of mobile
CC       elements that move relative to each other. The core element with
CC       the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and
CC       regions of RPB1 and RPB2 forming the active center. The clamp
CC       element (portions of RPB1, RPB2 and RPB3) is connected to the core
CC       through a set of flexible switches and moves to open and close the
CC       cleft. A bridging helix emanates from RPB1 and crosses the cleft
CC       near the catalytic site and is thought to promote translocation of
CC       Pol II by acting as a ratchet that moves the RNA-DNA hybrid
CC       through the active site by switching from straight to bent
CC       conformations at each step of nucleotide addition. In elongating
CC       Pol II, the lid loop (RPB1) appears to act as a wedge to drive
CC       apart the DNA and RNA strands at the upstream end of the
CC       transcription bubble and guide the RNA strand toward the RNA exit
CC       groove located near the base of the largely unstructured CTD
CC       domain of RPB1. The rudder loop (RPB1) interacts with single-
CC       stranded DNA after separation from the RNA strand, likely
CC       preventing reassociation with the exiting RNA. The cleft is
CC       surrounded by jaws: an upper jaw formed by portions of RBP1, RPB2
CC       and RPB9, and a lower jaw, formed by RPB5 and portions of RBP1.
CC       The jaws are thought to grab the incoming DNA template, mainly by
CC       RPB5 direct contacts to DNA.
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex
CC       consisting of 12 subunits. Interacts with ASK10, ESS1, RTT103 and
CC       SHE2. {ECO:0000269|PubMed:10531363, ECO:0000269|PubMed:11805306,
CC       ECO:0000269|PubMed:12914699, ECO:0000269|PubMed:14555478,
CC       ECO:0000269|PubMed:15565157, ECO:0000269|PubMed:16341226,
CC       ECO:0000269|PubMed:20713510}.
CC   -!- INTERACTION:
CC       Q06697:CDC73; NbExp=17; IntAct=EBI-15760, EBI-29913;
CC       P89105:CTR9; NbExp=4; IntAct=EBI-15760, EBI-5283;
CC       P53064:RTF1; NbExp=7; IntAct=EBI-15760, EBI-16303;
CC       Q00416:SEN1; NbExp=3; IntAct=EBI-15760, EBI-16945;
CC       P27692:SPT5; NbExp=3; IntAct=EBI-15760, EBI-17937;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DOMAIN: The C-terminal domain (CTD) serves as a platform for
CC       assembly of factors that regulate transcription initiation,
CC       elongation, termination and mRNA processing. {ECO:0000305}.
CC   -!- PTM: The tandem 7 residues repeats in the C-terminal domain (CTD)
CC       can be highly phosphorylated. The phosphorylation activates Pol
CC       II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5'
CC       of the heptapeptide repeat. The phosphorylated form of Pol II
CC       appears to carry, on average, one phosphate per repeat. The
CC       phosphorylation state is believed to result from the balanced
CC       action of site-specific CTD kinases and phosphataes, and a "CTD
CC       code" that specifies the position of Pol II within the
CC       transcription cycle has been proposed. Phosphorylation at 'Ser-5'
CC       occurs in promoter-proximal regions in early elongation.
CC       Phosphorylation at 'Ser-2' predominates in regions more distal to
CC       the promoter and triggers binding of the 3' RNA processing
CC       machinery. CTD kinases include KIN28 (as part of the TFKII
CC       complex, a subcomplex of the TFIIH holo complex), SSN3/SRB10 (as
CC       part of the SRB8-11 complex, a module of the Mediator complex),
CC       CTK1 (as part of CTD kinase), and probably BUR1 (as part of the
CC       BUR1-BUR2 kinase complex). Phosphatases include FCP1 and SSU72.
CC       {ECO:0000269|PubMed:11390638, ECO:0000269|PubMed:15047695,
CC       ECO:0000269|PubMed:9702190}.
CC   -!- MISCELLANEOUS: Mutagenesis experiments demonstrate that the
CC       minimum viable CTD contains eight consensus Y-S-P-T-S-P-[A-S-N-G]
CC       heptapeptide repeats. Identical and simultaneous substitutions in
CC       a number of consecutive repeats are lethal: 'Ser-2' -> 'Ala-2' (14
CC       repeats), 'Ser-5' -> 'Ala-5' (15 repeats), '2-Ser-Pro-Thr-Ser-5'->
CC       '2-Ala-Pro-Thr-Ala-5' (10 repeats), 'Ser-2'-> 'Glu-2' (15
CC       repeats), 'Ser-5' -> 'Glu-5' (12 repeats), '2-Ser-Pro-3' -> '2-
CC       Pro-Ser-3' (15 repeats) and 'Tyr-1' -> 'Phe-1' (12 repeats).
CC   -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the
CC       RNA polymerase II transcribing complex probably involves a two-
CC       step mechanism. The initial binding seems to occur at the entry
CC       (E) site and involves a magnesium ion temporarily coordinated by
CC       three conserved aspartate residues of the two largest RNA Pol II
CC       subunits. The ribonucleoside triphosphate is transferred by a
CC       rotation to the nucleotide addition (A) site for pairing with the
CC       template DNA. The catalytic A site involves three conserved
CC       aspartate residues of the RNA Pol II largest subunit which
CC       permanently coordinate a second magnesium ion.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000305}.
DR   EMBL; X03128; CAA26904.1; -; Genomic_DNA.
DR   EMBL; X96876; CAA65619.1; -; Genomic_DNA.
DR   EMBL; Z74188; CAA98713.1; -; Genomic_DNA.
DR   EMBL; U27182; AAC49058.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11718.1; -; Genomic_DNA.
DR   PIR; S67686; RNBY2L.
DR   RefSeq; NP_010141.1; NM_001180200.1.
DR   PDB; 1I3Q; X-ray; 3.10 A; A=1-1733.
DR   PDB; 1I50; X-ray; 2.80 A; A=1-1733.
DR   PDB; 1I6H; X-ray; 3.30 A; A=1-1733.
DR   PDB; 1K83; X-ray; 2.80 A; A=1-1733.
DR   PDB; 1NIK; X-ray; 4.10 A; A=1-1733.
DR   PDB; 1NT9; X-ray; 4.20 A; A=1-1733.
DR   PDB; 1PQV; X-ray; 3.80 A; A=1-1733.
DR   PDB; 1R5U; X-ray; 4.50 A; A=1-1733.
DR   PDB; 1R9S; X-ray; 4.25 A; A=1-1733.
DR   PDB; 1R9T; X-ray; 3.50 A; A=1-1733.
DR   PDB; 1SFO; X-ray; 3.61 A; A=1-1733.
DR   PDB; 1TWA; X-ray; 3.20 A; A=1-1733.
DR   PDB; 1TWC; X-ray; 3.00 A; A=1-1733.
DR   PDB; 1TWF; X-ray; 2.30 A; A=1-1733.
DR   PDB; 1TWG; X-ray; 3.30 A; A=1-1733.
DR   PDB; 1TWH; X-ray; 3.40 A; A=1-1733.
DR   PDB; 1WCM; X-ray; 3.80 A; A=1-1733.
DR   PDB; 1Y1V; X-ray; 3.80 A; A=1-1733.
DR   PDB; 1Y1W; X-ray; 4.00 A; A=1-1733.
DR   PDB; 1Y1Y; X-ray; 4.00 A; A=1-1733.
DR   PDB; 1Y77; X-ray; 4.50 A; A=1-1733.
DR   PDB; 2B63; X-ray; 3.80 A; A=1-1733.
DR   PDB; 2B8K; X-ray; 4.15 A; A=1-1733.
DR   PDB; 2E2H; X-ray; 3.95 A; A=1-1733.
DR   PDB; 2E2I; X-ray; 3.41 A; A=1-1733.
DR   PDB; 2E2J; X-ray; 3.50 A; A=1-1733.
DR   PDB; 2JA5; X-ray; 3.80 A; A=1-1733.
DR   PDB; 2JA6; X-ray; 4.00 A; A=1-1733.
DR   PDB; 2JA7; X-ray; 3.80 A; A/M=1-1733.
DR   PDB; 2JA8; X-ray; 3.80 A; A=1-1733.
DR   PDB; 2L0I; NMR; -; B=1675-1688.
DR   PDB; 2LO6; NMR; -; B=1675-1688.
DR   PDB; 2NVQ; X-ray; 2.90 A; A=1-1733.
DR   PDB; 2NVT; X-ray; 3.36 A; A=1-1733.
DR   PDB; 2NVX; X-ray; 3.60 A; A=1-1733.
DR   PDB; 2NVY; X-ray; 3.40 A; A=1-1733.
DR   PDB; 2NVZ; X-ray; 4.30 A; A=1-1733.
DR   PDB; 2R7Z; X-ray; 3.80 A; A=1-1733.
DR   PDB; 2R92; X-ray; 3.80 A; A=1-1733.
DR   PDB; 2R93; X-ray; 4.00 A; A=1-1733.
DR   PDB; 2VUM; X-ray; 3.40 A; A=1-1733.
DR   PDB; 2YU9; X-ray; 3.40 A; A=1-1733.
DR   PDB; 3CQZ; X-ray; 2.80 A; A=1-1733.
DR   PDB; 3FKI; X-ray; 3.88 A; A=1-1733.
DR   PDB; 3GTG; X-ray; 3.78 A; A=1-1733.
DR   PDB; 3GTJ; X-ray; 3.42 A; A=1-1733.
DR   PDB; 3GTK; X-ray; 3.80 A; A=1-1733.
DR   PDB; 3GTL; X-ray; 3.38 A; A=1-1733.
DR   PDB; 3GTM; X-ray; 3.80 A; A=1-1733.
DR   PDB; 3GTO; X-ray; 4.00 A; A=1-1733.
DR   PDB; 3GTP; X-ray; 3.90 A; A=1-1733.
DR   PDB; 3GTQ; X-ray; 3.80 A; A=1-1733.
DR   PDB; 3H3V; X-ray; 4.00 A; B=1-1733.
DR   PDB; 3HOU; X-ray; 3.20 A; A/M=1-1733.
DR   PDB; 3HOV; X-ray; 3.50 A; A=1-1733.
DR   PDB; 3HOW; X-ray; 3.60 A; A=1-1733.
DR   PDB; 3HOX; X-ray; 3.65 A; A=1-1733.
DR   PDB; 3HOY; X-ray; 3.40 A; A=1-1733.
DR   PDB; 3HOZ; X-ray; 3.65 A; A=1-1733.
DR   PDB; 3I4M; X-ray; 3.70 A; A=1-1733.
DR   PDB; 3I4N; X-ray; 3.90 A; A=1-1733.
DR   PDB; 3J0K; EM; 36.00 A; A=1-1455.
DR   PDB; 3J1N; EM; 16.00 A; A=1-1455.
DR   PDB; 3K1F; X-ray; 4.30 A; A=1-1733.
DR   PDB; 3K7A; X-ray; 3.80 A; A=1-1733.
DR   PDB; 3M3Y; X-ray; 3.18 A; A=1-1733.
DR   PDB; 3M4O; X-ray; 3.57 A; A=1-1733.
DR   PDB; 3PO2; X-ray; 3.30 A; A=1-1733.
DR   PDB; 3PO3; X-ray; 3.30 A; A=1-1733.
DR   PDB; 3QT1; X-ray; 4.30 A; A=1-1733.
DR   PDB; 3RZD; X-ray; 3.30 A; A=1-1733.
DR   PDB; 3RZO; X-ray; 3.00 A; A=1-1733.
DR   PDB; 3S14; X-ray; 2.85 A; A=1-1733.
DR   PDB; 3S15; X-ray; 3.30 A; A=1-1733.
DR   PDB; 3S16; X-ray; 3.24 A; A=1-1733.
DR   PDB; 3S17; X-ray; 3.20 A; A=1-1733.
DR   PDB; 3S1M; X-ray; 3.13 A; A=1-1733.
DR   PDB; 3S1N; X-ray; 3.10 A; A=1-1733.
DR   PDB; 3S1Q; X-ray; 3.30 A; A=1-1733.
DR   PDB; 3S1R; X-ray; 3.20 A; A=1-1733.
DR   PDB; 3S2D; X-ray; 3.20 A; A=1-1733.
DR   PDB; 3S2H; X-ray; 3.30 A; A=1-1733.
DR   PDB; 4A3B; X-ray; 3.50 A; A=1-1732.
DR   PDB; 4A3C; X-ray; 3.50 A; A=1-1732.
DR   PDB; 4A3D; X-ray; 3.40 A; A=1-1732.
DR   PDB; 4A3E; X-ray; 3.40 A; A=1-1732.
DR   PDB; 4A3F; X-ray; 3.50 A; A=1-1732.
DR   PDB; 4A3G; X-ray; 3.50 A; A=1-1732.
DR   PDB; 4A3I; X-ray; 3.80 A; A=1-1732.
DR   PDB; 4A3J; X-ray; 3.70 A; A=1-1732.
DR   PDB; 4A3K; X-ray; 3.50 A; A=1-1732.
DR   PDB; 4A3L; X-ray; 3.50 A; A=1-1732.
DR   PDB; 4A3M; X-ray; 3.90 A; A=1-1732.
DR   PDB; 4A93; X-ray; 3.40 A; A=1-1732.
DR   PDB; 4BBR; X-ray; 3.40 A; A=1-1733.
DR   PDB; 4BBS; X-ray; 3.60 A; A=1-1733.
DR   PDB; 4BXX; X-ray; 3.28 A; A=1-1733.
DR   PDB; 4BXZ; X-ray; 4.80 A; A=1-1733.
DR   PDB; 4BY1; X-ray; 3.60 A; A=1-1733.
DR   PDB; 4BY7; X-ray; 3.15 A; A=1-1733.
DR   PDB; 4GWQ; X-ray; 4.50 A; H=1619-1653.
DR   PDB; 4V1M; EM; 6.60 A; A=1-1733.
DR   PDB; 4V1N; EM; 7.80 A; A=1-1733.
DR   PDB; 4V1O; EM; 9.70 A; A=1-1733.
DR   PDB; 4X67; X-ray; 4.10 A; A=1-1733.
DR   PDB; 4X6A; X-ray; 3.96 A; A=1-1733.
DR   PDB; 4Y52; X-ray; 3.50 A; A=1-1733.
DR   PDB; 4Y7N; X-ray; 3.30 A; A=1-1733.
DR   PDB; 5C3E; X-ray; 3.70 A; A=1-1733.
DR   PDB; 5C44; X-ray; 3.95 A; A=1-1733.
DR   PDB; 5C4A; X-ray; 4.20 A; A=1-1733.
DR   PDB; 5C4J; X-ray; 4.00 A; A=1-1733.
DR   PDB; 5C4X; X-ray; 4.00 A; A=1-1733.
DR   PDB; 5FMF; EM; 6.00 A; A=1-1733.
DR   PDB; 5FYW; EM; 4.35 A; A=1-1733.
DR   PDB; 5FZ5; EM; 8.80 A; A=1-1733.
DR   PDB; 5IP7; X-ray; 3.52 A; A=2-1733.
DR   PDB; 5IP9; X-ray; 3.90 A; A=2-1733.
DR   PDB; 5LVF; NMR; -; B=1673-1688.
DR   PDB; 5SVA; EM; 15.30 A; A=1-1733, k=1666-1690.
DR   PDB; 5U5Q; X-ray; 3.80 A; A=1-1733.
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; 2L0I; -.
DR   PDBsum; 2LO6; -.
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; 4GWQ; -.
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; 5LVF; -.
DR   PDBsum; 5SVA; -.
DR   PDBsum; 5U5Q; -.
DR   ProteinModelPortal; P04050; -.
DR   SMR; P04050; -.
DR   BioGrid; 31921; 679.
DR   DIP; DIP-611N; -.
DR   IntAct; P04050; 44.
DR   MINT; MINT-432838; -.
DR   STRING; 4932.YDL140C; -.
DR   iPTMnet; P04050; -.
DR   MaxQB; P04050; -.
DR   PRIDE; P04050; -.
DR   TopDownProteomics; P04050; -.
DR   EnsemblFungi; YDL140C; YDL140C; YDL140C.
DR   GeneID; 851415; -.
DR   KEGG; sce:YDL140C; -.
DR   EuPathDB; FungiDB:YDL140C; -.
DR   SGD; S000002299; RPO21.
DR   GeneTree; ENSGT00870000136522; -.
DR   HOGENOM; HOG000222975; -.
DR   InParanoid; P04050; -.
DR   KO; K03006; -.
DR   OMA; MPDFDPT; -.
DR   OrthoDB; EOG092C01XQ; -.
DR   BioCyc; YEAST:G3O-29539-MONOMER; -.
DR   BRENDA; 2.7.7.6; 984.
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-72086; mRNA Capping.
DR   Reactome; R-SCE-72165; mRNA Splicing - Minor Pathway.
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   EvolutionaryTrace; P04050; -.
DR   PRO; PR:P04050; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR   GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:CACAO.
DR   GO; GO:0005773; C:vacuole; IEA:EnsemblPlants.
DR   GO; GO:0003677; F:DNA binding; IDA:SGD.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IMP:SGD.
DR   GO; GO:0001172; P:transcription, RNA-templated; IEA:GOC.
DR   GO; GO:0019985; P:translesion synthesis; IMP:SGD.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR000684; RNA_pol_II_repeat_euk.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR007075; RNA_pol_Rpb1_6.
DR   InterPro; IPR007073; RNA_pol_Rpb1_7.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR   Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR   Pfam; PF05001; RNA_pol_Rpb1_R; 12.
DR   SMART; SM00663; RPOLA_N; 1.
DR   PROSITE; PS00115; RNA_POL_II_REPEAT; 22.
PE   1: Evidence at protein level;
DR   PRODOM; P04050.
DR   SWISS-2DPAGE; P04050.
KW   3D-structure; Complete proteome; DNA-binding;
KW   DNA-directed RNA polymerase; Isopeptide bond; Magnesium;
KW   Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transferase;
KW   Ubl conjugation; Zinc.
FT   CHAIN         1   1733       DNA-directed RNA polymerase II subunit
FT                                RPB1.
FT                                /FTId=PRO_0000073946.
FT   REPEAT     1549   1555       1.
FT   REPEAT     1556   1562       2.
FT   REPEAT     1563   1569       3.
FT   REPEAT     1570   1576       4.
FT   REPEAT     1577   1583       5.
FT   REPEAT     1584   1590       6.
FT   REPEAT     1591   1597       7.
FT   REPEAT     1598   1604       8.
FT   REPEAT     1605   1611       9.
FT   REPEAT     1612   1618       10.
FT   REPEAT     1619   1625       11.
FT   REPEAT     1626   1632       12.
FT   REPEAT     1633   1639       13.
FT   REPEAT     1640   1646       14.
FT   REPEAT     1647   1653       15.
FT   REPEAT     1654   1660       16.
FT   REPEAT     1661   1667       17.
FT   REPEAT     1668   1674       18.
FT   REPEAT     1675   1681       19.
FT   REPEAT     1682   1688       20.
FT   REPEAT     1689   1695       21.
FT   REPEAT     1696   1702       22.
FT   REPEAT     1703   1709       23.
FT   REPEAT     1710   1716       24; approximate.
FT   REGION      248    260       Lid loop.
FT   REGION      306    323       Rudder loop.
FT   REGION      810    822       Bridging helix.
FT   REGION     1549   1716       C-terminal domain (CTD); 24 X 7 AA
FT                                approximate tandem repeats of Y-S-P-T-S-
FT                                P-[A-S-N-G].
FT   METAL        67     67       Zinc 1. {ECO:0000244|PDB:4BBR,
FT                                ECO:0000244|PDB:4V1M,
FT                                ECO:0000269|PubMed:23151482,
FT                                ECO:0000269|PubMed:25652824}.
FT   METAL        70     70       Zinc 1. {ECO:0000244|PDB:4BBR,
FT                                ECO:0000244|PDB:4V1M,
FT                                ECO:0000269|PubMed:23151482,
FT                                ECO:0000269|PubMed:25652824}.
FT   METAL        77     77       Zinc 1. {ECO:0000244|PDB:4BBR,
FT                                ECO:0000244|PDB:4V1M,
FT                                ECO:0000269|PubMed:23151482,
FT                                ECO:0000269|PubMed:25652824}.
FT   METAL        80     80       Zinc 1; via tele nitrogen.
FT                                {ECO:0000244|PDB:4BBR,
FT                                ECO:0000244|PDB:4V1M,
FT                                ECO:0000269|PubMed:23151482,
FT                                ECO:0000269|PubMed:25652824}.
FT   METAL       107    107       Zinc 2. {ECO:0000244|PDB:4BBR,
FT                                ECO:0000244|PDB:4V1M,
FT                                ECO:0000269|PubMed:23151482,
FT                                ECO:0000269|PubMed:25652824}.
FT   METAL       110    110       Zinc 2. {ECO:0000244|PDB:4BBR,
FT                                ECO:0000244|PDB:4V1M,
FT                                ECO:0000269|PubMed:23151482,
FT                                ECO:0000269|PubMed:25652824}.
FT   METAL       148    148       Zinc 2. {ECO:0000244|PDB:4BBR,
FT                                ECO:0000244|PDB:4V1M,
FT                                ECO:0000269|PubMed:23151482,
FT                                ECO:0000269|PubMed:25652824}.
FT   METAL       167    167       Zinc 2. {ECO:0000244|PDB:4BBR,
FT                                ECO:0000244|PDB:4V1M,
FT                                ECO:0000269|PubMed:23151482,
FT                                ECO:0000269|PubMed:25652824}.
FT   METAL       481    481       Magnesium 1; catalytic.
FT                                {ECO:0000244|PDB:4BBR,
FT                                ECO:0000244|PDB:4V1M,
FT                                ECO:0000269|PubMed:23151482,
FT                                ECO:0000269|PubMed:25652824}.
FT   METAL       481    481       Magnesium 2; shared with RPB2.
FT                                {ECO:0000244|PDB:4BBR,
FT                                ECO:0000244|PDB:4V1M,
FT                                ECO:0000269|PubMed:23151482,
FT                                ECO:0000269|PubMed:25652824}.
FT   METAL       483    483       Magnesium 1; catalytic.
FT                                {ECO:0000244|PDB:4BBR,
FT                                ECO:0000244|PDB:4V1M,
FT                                ECO:0000269|PubMed:23151482,
FT                                ECO:0000269|PubMed:25652824}.
FT   METAL       483    483       Magnesium 2; shared with RPB2.
FT                                {ECO:0000244|PDB:4BBR,
FT                                ECO:0000244|PDB:4V1M,
FT                                ECO:0000269|PubMed:23151482,
FT                                ECO:0000269|PubMed:25652824}.
FT   METAL       485    485       Magnesium 1; catalytic.
FT                                {ECO:0000244|PDB:4BBR,
FT                                ECO:0000244|PDB:4V1M,
FT                                ECO:0000269|PubMed:23151482,
FT                                ECO:0000269|PubMed:25652824}.
FT   MOD_RES    1471   1471       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18407956}.
FT   CROSSLNK    695    695       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000244|PubMed:22106047}.
FT   CROSSLNK   1246   1246       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000244|PubMed:22106047}.
FT   CROSSLNK   1350   1350       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000244|PubMed:22106047}.
FT   VARIANT    1653   1659       Missing (in strain: A364A).
FT   CONFLICT   1514   1514       A -> V (in Ref. 1; CAA26904).
FT                                {ECO:0000305}.
FT   CONFLICT   1524   1524       G -> A (in Ref. 1; CAA26904).
FT                                {ECO:0000305}.
FT   CONFLICT   1601   1601       T -> M (in Ref. 1). {ECO:0000305}.
FT   STRAND       16     18       {ECO:0000244|PDB:1TWF}.
FT   HELIX        24     29       {ECO:0000244|PDB:1TWF}.
FT   STRAND       32     34       {ECO:0000244|PDB:4BXX}.
FT   STRAND       39     41       {ECO:0000244|PDB:2NVT}.
FT   STRAND       43     45       {ECO:0000244|PDB:1TWC}.
FT   STRAND       46     48       {ECO:0000244|PDB:3S14}.
FT   STRAND       51     54       {ECO:0000244|PDB:1TWF}.
FT   STRAND       56     58       {ECO:0000244|PDB:1TWF}.
FT   STRAND       62     64       {ECO:0000244|PDB:3CQZ}.
FT   STRAND       67     69       {ECO:0000244|PDB:1TWF}.
FT   TURN         74     76       {ECO:0000244|PDB:1I50}.
FT   STRAND       84     91       {ECO:0000244|PDB:1TWF}.
FT   HELIX        93     95       {ECO:0000244|PDB:1TWF}.
FT   HELIX        96    105       {ECO:0000244|PDB:1TWF}.
FT   TURN        108    110       {ECO:0000244|PDB:1TWF}.
FT   STRAND      113    115       {ECO:0000244|PDB:1I50}.
FT   STRAND      117    119       {ECO:0000244|PDB:2NVQ}.
FT   HELIX       120    126       {ECO:0000244|PDB:1TWF}.
FT   STRAND      127    129       {ECO:0000244|PDB:2E2I}.
FT   HELIX       131    142       {ECO:0000244|PDB:1TWF}.
FT   STRAND      150    152       {ECO:0000244|PDB:1TWF}.
FT   STRAND      160    163       {ECO:0000244|PDB:1I50}.
FT   STRAND      173    177       {ECO:0000244|PDB:1I50}.
FT   STRAND      181    185       {ECO:0000244|PDB:1TWF}.
FT   STRAND      187    190       {ECO:0000244|PDB:1TWF}.
FT   STRAND      198    202       {ECO:0000244|PDB:1TWF}.
FT   HELIX       204    211       {ECO:0000244|PDB:1TWF}.
FT   STRAND      212    214       {ECO:0000244|PDB:3S2H}.
FT   HELIX       216    221       {ECO:0000244|PDB:1TWF}.
FT   TURN        226    228       {ECO:0000244|PDB:1TWF}.
FT   HELIX       231    234       {ECO:0000244|PDB:1TWF}.
FT   STRAND      235    239       {ECO:0000244|PDB:1TWF}.
FT   TURN        244    246       {ECO:0000244|PDB:1TWF}.
FT   STRAND      253    255       {ECO:0000244|PDB:1TWF}.
FT   STRAND      257    260       {ECO:0000244|PDB:4BBR}.
FT   HELIX       261    280       {ECO:0000244|PDB:1TWF}.
FT   TURN        281    283       {ECO:0000244|PDB:3CQZ}.
FT   HELIX       286    304       {ECO:0000244|PDB:1TWF}.
FT   STRAND      307    310       {ECO:0000244|PDB:3S14}.
FT   STRAND      313    316       {ECO:0000244|PDB:4BBR}.
FT   STRAND      318    321       {ECO:0000244|PDB:3S14}.
FT   HELIX       325    329       {ECO:0000244|PDB:1I50}.
FT   TURN        330    335       {ECO:0000244|PDB:1TWF}.
FT   HELIX       338    340       {ECO:0000244|PDB:1TWF}.
FT   STRAND      341    344       {ECO:0000244|PDB:4Y7N}.
FT   STRAND      347    355       {ECO:0000244|PDB:1TWF}.
FT   STRAND      363    367       {ECO:0000244|PDB:1TWF}.
FT   HELIX       368    371       {ECO:0000244|PDB:1TWF}.
FT   STRAND      375    379       {ECO:0000244|PDB:1TWF}.
FT   TURN        382    384       {ECO:0000244|PDB:1TWF}.
FT   HELIX       385    394       {ECO:0000244|PDB:1TWF}.
FT   TURN        395    397       {ECO:0000244|PDB:1TWF}.
FT   STRAND      398    400       {ECO:0000244|PDB:1TWF}.
FT   STRAND      402    406       {ECO:0000244|PDB:1TWF}.
FT   HELIX       408    410       {ECO:0000244|PDB:3S14}.
FT   STRAND      412    414       {ECO:0000244|PDB:1TWF}.
FT   TURN        415    417       {ECO:0000244|PDB:3CQZ}.
FT   TURN        419    422       {ECO:0000244|PDB:1TWF}.
FT   STRAND      431    435       {ECO:0000244|PDB:1TWF}.
FT   STRAND      441    445       {ECO:0000244|PDB:1TWF}.
FT   HELIX       452    454       {ECO:0000244|PDB:1TWF}.
FT   STRAND      455    470       {ECO:0000244|PDB:1TWF}.
FT   HELIX       472    474       {ECO:0000244|PDB:1TWF}.
FT   HELIX       475    478       {ECO:0000244|PDB:1TWF}.
FT   STRAND      482    484       {ECO:0000244|PDB:1TWF}.
FT   STRAND      486    490       {ECO:0000244|PDB:1TWF}.
FT   HELIX       495    504       {ECO:0000244|PDB:1TWF}.
FT   HELIX       507    510       {ECO:0000244|PDB:1TWF}.
FT   STRAND      511    513       {ECO:0000244|PDB:1TWF}.
FT   TURN        514    517       {ECO:0000244|PDB:1TWF}.
FT   STRAND      518    520       {ECO:0000244|PDB:1TWF}.
FT   HELIX       525    535       {ECO:0000244|PDB:1TWF}.
FT   STRAND      536    538       {ECO:0000244|PDB:3S1N}.
FT   STRAND      540    542       {ECO:0000244|PDB:1TWF}.
FT   HELIX       543    552       {ECO:0000244|PDB:1TWF}.
FT   STRAND      553    555       {ECO:0000244|PDB:3CQZ}.
FT   STRAND      567    569       {ECO:0000244|PDB:1TWF}.
FT   STRAND      571    573       {ECO:0000244|PDB:1TWF}.
FT   HELIX       574    581       {ECO:0000244|PDB:1TWF}.
FT   STRAND      588    590       {ECO:0000244|PDB:1TWF}.
FT   STRAND      596    598       {ECO:0000244|PDB:2E2I}.
FT   STRAND      600    602       {ECO:0000244|PDB:3PO2}.
FT   STRAND      604    608       {ECO:0000244|PDB:1TWF}.
FT   STRAND      611    615       {ECO:0000244|PDB:1TWF}.
FT   HELIX       619    622       {ECO:0000244|PDB:1TWF}.
FT   STRAND      626    628       {ECO:0000244|PDB:1I50}.
FT   HELIX       629    637       {ECO:0000244|PDB:1TWF}.
FT   HELIX       639    658       {ECO:0000244|PDB:1TWF}.
FT   HELIX       666    669       {ECO:0000244|PDB:1TWF}.
FT   HELIX       673    699       {ECO:0000244|PDB:1TWF}.
FT   STRAND      706    708       {ECO:0000244|PDB:1I50}.
FT   HELIX       710    736       {ECO:0000244|PDB:1TWF}.
FT   HELIX       742    749       {ECO:0000244|PDB:1TWF}.
FT   STRAND      750    752       {ECO:0000244|PDB:1K83}.
FT   HELIX       755    762       {ECO:0000244|PDB:1TWF}.
FT   STRAND      770    774       {ECO:0000244|PDB:1I3Q}.
FT   STRAND      778    781       {ECO:0000244|PDB:4BBR}.
FT   STRAND      782    784       {ECO:0000244|PDB:1TWF}.
FT   TURN        794    798       {ECO:0000244|PDB:1TWF}.
FT   TURN        804    806       {ECO:0000244|PDB:1TWF}.
FT   HELIX       810    845       {ECO:0000244|PDB:1TWF}.
FT   STRAND      863    867       {ECO:0000244|PDB:1TWF}.
FT   HELIX       868    870       {ECO:0000244|PDB:1TWF}.
FT   HELIX       875    877       {ECO:0000244|PDB:1TWF}.
FT   STRAND      878    882       {ECO:0000244|PDB:1TWF}.
FT   HELIX       884    886       {ECO:0000244|PDB:1TWF}.
FT   HELIX       890    897       {ECO:0000244|PDB:1TWF}.
FT   STRAND      901    903       {ECO:0000244|PDB:2YU9}.
FT   TURN        904    906       {ECO:0000244|PDB:1TWF}.
FT   TURN        910    912       {ECO:0000244|PDB:1TWF}.
FT   STRAND      913    915       {ECO:0000244|PDB:3S15}.
FT   HELIX       916    919       {ECO:0000244|PDB:1TWF}.
FT   HELIX       923    946       {ECO:0000244|PDB:1TWF}.
FT   TURN        947    949       {ECO:0000244|PDB:1TWF}.
FT   STRAND      953    958       {ECO:0000244|PDB:1TWF}.
FT   HELIX       960    970       {ECO:0000244|PDB:1TWF}.
FT   STRAND      975    977       {ECO:0000244|PDB:1K83}.
FT   HELIX       983    994       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1005   1013       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1016   1025       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1028   1033       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1039   1056       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1064   1076       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1079   1082       {ECO:0000244|PDB:3S1Q}.
FT   HELIX      1086   1088       {ECO:0000244|PDB:2NVQ}.
FT   STRAND     1089   1091       {ECO:0000244|PDB:3CQZ}.
FT   STRAND     1092   1094       {ECO:0000244|PDB:3S1Q}.
FT   HELIX      1097   1104       {ECO:0000244|PDB:1TWF}.
FT   TURN       1105   1107       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1115   1120       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1122   1126       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1128   1138       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1143   1145       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1147   1154       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1158   1160       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1164   1166       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1167   1171       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1172   1174       {ECO:0000244|PDB:1I50}.
FT   STRAND     1179   1182       {ECO:0000244|PDB:4BY7}.
FT   STRAND     1190   1197       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1199   1204       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1209   1220       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1221   1223       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1224   1228       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1233   1235       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1237   1242       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1258   1270       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1272   1275       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1282   1292       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1296   1310       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1313   1316       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1317   1322       {ECO:0000244|PDB:3M3Y}.
FT   TURN       1324   1326       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1328   1330       {ECO:0000244|PDB:1I50}.
FT   HELIX      1332   1339       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1341   1357       {ECO:0000244|PDB:1TWF}.
FT   TURN       1358   1360       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1365   1374       {ECO:0000244|PDB:1TWF}.
FT   TURN       1375   1377       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1378   1380       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1384   1386       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1388   1390       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1392   1394       {ECO:0000244|PDB:3S14}.
FT   HELIX      1396   1399       {ECO:0000244|PDB:3S14}.
FT   TURN       1400   1402       {ECO:0000244|PDB:3S14}.
FT   HELIX      1406   1415       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1424   1429       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1437   1439       {ECO:0000244|PDB:1TWF}.
FT   STRAND     1440   1445       {ECO:0000244|PDB:1TWF}.
FT   HELIX      1447   1450       {ECO:0000244|PDB:4BY7}.
FT   STRAND     1677   1680       {ECO:0000244|PDB:2LO6}.
SQ   SEQUENCE   1733 AA;  191612 MW;  A45C1360FF99F968 CRC64;
     MVGQQYSSAP LRTVKEVQFG LFSPEEVRAI SVAKIRFPET MDETQTRAKI GGLNDPRLGS
     IDRNLKCQTC QEGMNECPGH FGHIDLAKPV FHVGFIAKIK KVCECVCMHC GKLLLDEHNE
     LMRQALAIKD SKKRFAAIWT LCKTKMVCET DVPSEDDPTQ LVSRGGCGNT QPTIRKDGLK
     LVGSWKKDRA TGDADEPELR VLSTEEILNI FKHISVKDFT SLGFNEVFSR PEWMILTCLP
     VPPPPVRPSI SFNESQRGED DLTFKLADIL KANISLETLE HNGAPHHAIE EAESLLQFHV
     ATYMDNDIAG QPQALQKSGR PVKSIRARLK GKEGRIRGNL MGKRVDFSAR TVISGDPNLE
     LDQVGVPKSI AKTLTYPEVV TPYNIDRLTQ LVRNGPNEHP GAKYVIRDSG DRIDLRYSKR
     AGDIQLQYGW KVERHIMDND PVLFNRQPSL HKMSMMAHRV KVIPYSTFRL NLSVTSPYNA
     DFDGDEMNLH VPQSEETRAE LSQLCAVPLQ IVSPQSNKPC MGIVQDTLCG IRKLTLRDTF
     IELDQVLNML YWVPDWDGVI PTPAIIKPKP LWSGKQILSV AIPNGIHLQR FDEGTTLLSP
     KDNGMLIIDG QIIFGVVEKK TVGSSNGGLI HVVTREKGPQ VCAKLFGNIQ KVVNFWLLHN
     GFSTGIGDTI ADGPTMREIT ETIAEAKKKV LDVTKEAQAN LLTAKHGMTL RESFEDNVVR
     FLNEARDKAG RLAEVNLKDL NNVKQMVMAG SKGSFINIAQ MSACVGQQSV EGKRIAFGFV
     DRTLPHFSKD DYSPESKGFV ENSYLRGLTP QEFFFHAMGG REGLIDTAVK TAETGYIQRR
     LVKALEDIMV HYDNTTRNSL GNVIQFIYGE DGMDAAHIEK QSLDTIGGSD AAFEKRYRVD
     LLNTDHTLDP SLLESGSEIL GDLKLQVLLD EEYKQLVKDR KFLREVFVDG EANWPLPVNI
     RRIIQNAQQT FHIDHTKPSD LTIKDIVLGV KDLQENLLVL RGKNEIIQNA QRDAVTLFCC
     LLRSRLATRR VLQEYRLTKQ AFDWVLSNIE AQFLRSVVHP GEMVGVLAAQ SIGEPATQMT
     LNTFHFAGVA SKKVTSGVPR LKEILNVAKN MKTPSLTVYL EPGHAADQEQ AKLIRSAIEH
     TTLKSVTIAS EIYYDPDPRS TVIPEDEEII QLHFSLLDEE AEQSFDQQSP WLLRLELDRA
     AMNDKDLTMG QVGERIKQTF KNDLFVIWSE DNDEKLIIRC RVVRPKSLDA ETEAEEDHML
     KKIENTMLEN ITLRGVENIE RVVMMKYDRK VPSPTGEYVK EPEWVLETDG VNLSEVMTVP
     GIDPTRIYTN SFIDIMEVLG IEAGRAALYK EVYNVIASDG SYVNYRHMAL LVDVMTTQGG
     LTSVTRHGFN RSNTGALMRC SFEETVEILF EAGASAELDD CRGVSENVIL GQMAPIGTGA
     FDVMIDEESL VKYMPEQKIT EIEDGQDGGV TPYSNESGLV NADLDVKDEL MFSPLVDSGS
     NDAMAGGFTA YGGADYGEAT SPFGAYGEAP TSPGFGVSSP GFSPTSPTYS PTSPAYSPTS
     PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS
     PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPA YSPTSPSYSP TSPSYSPTSP
     SYSPTSPSYS PTSPNYSPTS PSYSPTSPGY SPGSPAYSPK QDEQKHNENE NSR
//

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