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 03-AUG-2022, entry version 236.
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; Saccharomycetes;
OC 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., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., 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., 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] 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; DOI=10.1093/genetics/140.4.1223;
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., 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., Young R.A.,
RA Greenblatt J.;
RT "An unusual eukaryotic protein phosphatase required for transcription by
RT 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 the
RT 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 BY
RP 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 to
RT 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., Greenblatt J.F.,
RA 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 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 [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 factor
RT 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 LYS-1350,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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., 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 [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 complex
RT 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 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 [23]
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 [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: implications
RT 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 in the
RT 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 cocrystal at
RT 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, 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 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 [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 updated
RT structural model.";
RL Structure 14:973-982(2006).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND 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 II-
RT TFIIB complex.";
RL Nature 493:437-440(2013).
RN [33]
RP STRUCTURE BY ELECTRON MICROSCOPY (6.60 ANGSTROMS) IN COMPLEX WITH MAGNESIUM
RP AND ZINC.
RX PubMed=25652824; DOI=10.1038/nature14229;
RA Plaschka C., Lariviere L., Wenzeck L., Seizl M., Hemann M., Tegunov D.,
RA Petrotchenko E.V., Borchers C.H., Baumeister W., Herzog F., Villa E.,
RA Cramer P.;
RT "Architecture of the RNA polymerase II-Mediator core initiation complex.";
RL Nature 518:376-380(2015).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Largest and catalytic component of RNA polymerase II which synthesizes
CC mRNA precursors and many functional non-coding RNAs. Forms the
CC polymerase active center together with the second largest subunit. Pol
CC II is the central component of the basal RNA polymerase II
CC transcription machinery. During a transcription cycle, Pol II, general
CC transcription factors and the Mediator complex assemble as the
CC preinitiation complex (PIC) at the promoter. 11-15 base pairs of DNA
CC surrounding the transcription start site are melted and the single-
CC stranded DNA template strand of the promoter is positioned deeply
CC within the central active site cleft of Pol II to form the open
CC complex. After synthesis of about 30 bases of RNA, Pol II releases its
CC contacts with the core promoter and the rest of the transcription
CC machinery (promoter clearance) and enters the stage of transcription
CC elongation in which it moves on the template as the transcript
CC elongates. Pol II appears to oscillate between inactive and active
CC conformations at each step of nucleotide addition. Elongation is
CC influenced by the phosphorylation status of the C-terminal domain (CTD)
CC of Pol II largest subunit (RPB1), which serves as a platform for
CC assembly of factors that regulate transcription initiation, elongation,
CC termination and mRNA processing. Pol II is composed of mobile elements
CC that move relative to each other. The core element with the central
CC large cleft comprises RPB3, RBP10, RPB11, RPB12 and regions of RPB1 and
CC RPB2 forming the active center. The clamp element (portions of RPB1,
CC RPB2 and RPB3) is connected to the core through a set of flexible
CC switches and moves to open and close the cleft. A bridging helix
CC emanates from RPB1 and crosses the cleft near the catalytic site and is
CC thought to promote translocation of Pol II by acting as a ratchet that
CC moves the RNA-DNA hybrid through the active site by switching from
CC straight to bent conformations at each step of nucleotide addition. In
CC elongating Pol II, the lid loop (RPB1) appears to act as a wedge to
CC drive 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 domain of
CC RPB1. The rudder loop (RPB1) interacts with single-stranded DNA after
CC separation from the RNA strand, likely preventing reassociation with
CC the exiting RNA. The cleft is surrounded by jaws: an upper jaw formed
CC by portions of RBP1, RPB2 and RPB9, and a lower jaw, formed by RPB5 and
CC portions of RBP1. The jaws are thought to grab the incoming DNA
CC template, mainly by RPB5 direct contacts to DNA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6;
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex consisting
CC of 12 subunits. Interacts with ASK10, ESS1, RTT103 and SHE2.
CC {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 P04050; Q06697: CDC73; NbExp=17; IntAct=EBI-15760, EBI-29913;
CC P04050; P89105: CTR9; NbExp=4; IntAct=EBI-15760, EBI-5283;
CC P04050; P53617: NRD1; NbExp=2; IntAct=EBI-15760, EBI-12228;
CC P04050; P08518: RPB2; NbExp=4; IntAct=EBI-15760, EBI-15767;
CC P04050; P53064: RTF1; NbExp=7; IntAct=EBI-15760, EBI-16303;
CC P04050; Q00416: SEN1; NbExp=4; IntAct=EBI-15760, EBI-16945;
CC P04050; 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 assembly
CC of factors that regulate transcription initiation, elongation,
CC termination and mRNA processing. {ECO:0000305}.
CC -!- PTM: The tandem 7 residues repeats in the C-terminal domain (CTD) can
CC be highly phosphorylated. The phosphorylation activates Pol II.
CC Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the
CC heptapeptide repeat. The phosphorylated form of Pol II appears to
CC carry, on average, one phosphate per repeat. The phosphorylation state
CC is believed to result from the balanced action of site-specific CTD
CC kinases and phosphatases, and a 'CTD code' that specifies the position
CC of Pol II within the transcription cycle has been proposed.
CC Phosphorylation at 'Ser-5' occurs in promoter-proximal regions in early
CC elongation. Phosphorylation at 'Ser-2' predominates in regions more
CC distal to the promoter and triggers binding of the 3' RNA processing
CC machinery. CTD kinases include KIN28 (as part of the TFKII complex, a
CC subcomplex of the TFIIH holo complex), SSN3/SRB10 (as part of the SRB8-
CC 11 complex, a module of the Mediator complex), CTK1 (as part of CTD
CC kinase), and probably BUR1 (as part of the BUR1-BUR2 kinase complex).
CC Phosphatases include FCP1 and SSU72. {ECO:0000269|PubMed:11390638,
CC ECO:0000269|PubMed:15047695, ECO:0000269|PubMed:9702190}.
CC -!- MISCELLANEOUS: Mutagenesis experiments demonstrate that the minimum
CC viable CTD contains eight consensus Y-S-P-T-S-P-[A-S-N-G] heptapeptide
CC repeats. Identical and simultaneous substitutions in a number of
CC consecutive repeats are lethal: 'Ser-2' -> 'Ala-2' (14 repeats), 'Ser-
CC 5' -> 'Ala-5' (15 repeats), '2-Ser-Pro-Thr-Ser-5'-> '2-Ala-Pro-Thr-Ala-
CC 5' (10 repeats), 'Ser-2'-> 'Glu-2' (15 repeats), 'Ser-5' -> 'Glu-5' (12
CC repeats), '2-Ser-Pro-3' -> '2-Pro-Ser-3' (15 repeats) and 'Tyr-1' ->
CC 'Phe-1' (12 repeats).
CC -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the RNA
CC polymerase II transcribing complex probably involves a two-step
CC mechanism. The initial binding seems to occur at the entry (E) site and
CC involves a magnesium ion temporarily coordinated by three conserved
CC aspartate residues of the two largest RNA Pol II subunits. The
CC ribonucleoside triphosphate is transferred by a rotation to the
CC nucleotide addition (A) site for pairing with the template DNA. The
CC catalytic A site involves three conserved aspartate residues of the RNA
CC Pol II largest subunit which permanently coordinate a second magnesium
CC ion.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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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; 5M9D; NMR; -; B=1678-1693.
DR PDB; 5OQJ; EM; 4.70 A; A=1-1733.
DR PDB; 5OQM; EM; 5.80 A; A=1-1733.
DR PDB; 5OT2; X-ray; 3.20 A; A=1-1733.
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 PDB; 5VKL; X-ray; 2.20 A; B=1476-1498.
DR PDB; 5VKO; X-ray; 1.80 A; B=1468-1500.
DR PDB; 5VVR; EM; 5.80 A; A=1-1733.
DR PDB; 5VVS; EM; 6.40 A; A=1-1733.
DR PDB; 5W4U; X-ray; 3.60 A; A=1-1733.
DR PDB; 5W51; X-ray; 3.40 A; A=1-1733.
DR PDB; 6BLO; X-ray; 3.40 A; A=1-1733.
DR PDB; 6BLP; X-ray; 3.20 A; A=1-1733.
DR PDB; 6BM2; X-ray; 3.40 A; A=1-1733.
DR PDB; 6BM4; X-ray; 2.95 A; A=1-1733.
DR PDB; 6BQF; X-ray; 3.35 A; A=1-1733.
DR PDB; 6GYK; EM; 5.10 A; A=1-1733.
DR PDB; 6GYL; EM; 4.80 A; A=1-1733.
DR PDB; 6GYM; EM; 6.70 A; A=1-1733.
DR PDB; 6I84; EM; 4.40 A; A=1-1733.
DR PDB; 6NPW; X-ray; 2.49 A; E=1672-1690.
DR PDB; 6O6C; EM; 3.10 A; A=1-1733.
DR PDB; 6UPX; X-ray; 3.40 A; A=1-1733.
DR PDB; 6UPY; X-ray; 3.40 A; A=1-1733.
DR PDB; 6UPZ; X-ray; 3.10 A; A=1-1733.
DR PDB; 6UQ0; X-ray; 3.56 A; A=1-1733.
DR PDB; 6UQ1; X-ray; 3.60 A; A=1-1733.
DR PDB; 6UQ2; X-ray; 3.20 A; A=1-1733.
DR PDB; 6UQ3; X-ray; 3.47 A; A=1-1733.
DR PDB; 7KED; X-ray; 3.60 A; A=1-1733.
DR PDB; 7KEE; X-ray; 3.45 A; A=1-1733.
DR PDB; 7KEF; X-ray; 3.89 A; A=1-1733.
DR PDB; 7NKX; EM; 2.90 A; A=1-1733.
DR PDB; 7NKY; EM; 3.20 A; A=1-1733.
DR PDB; 7O4I; EM; 3.20 A; A=1-1733.
DR PDB; 7O4J; EM; 2.90 A; A=1-1733.
DR PDB; 7O4K; EM; 3.60 A; A=1-1733.
DR PDB; 7O4L; EM; 3.40 A; A=1-1733.
DR PDB; 7O72; EM; 3.40 A; A=1-1733.
DR PDB; 7O73; EM; 3.40 A; A=1-1733.
DR PDB; 7O75; EM; 3.20 A; A=1-1733.
DR PDB; 7RIM; X-ray; 2.90 A; A=1-1733.
DR PDB; 7RIP; X-ray; 3.30 A; A=1-1733.
DR PDB; 7RIQ; X-ray; 3.00 A; A=1-1733.
DR PDB; 7RIW; X-ray; 3.20 A; A=1-1733.
DR PDB; 7RIX; X-ray; 3.40 A; A=1-1733.
DR PDB; 7RIY; X-ray; 3.70 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; 5M9D; -.
DR PDBsum; 5OQJ; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5OT2; -.
DR PDBsum; 5SVA; -.
DR PDBsum; 5U5Q; -.
DR PDBsum; 5VKL; -.
DR PDBsum; 5VKO; -.
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; 6NPW; -.
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; 7O4K; -.
DR PDBsum; 7O4L; -.
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; P04050; -.
DR SASBDB; P04050; -.
DR SMR; P04050; -.
DR BioGRID; 31921; 831.
DR ComplexPortal; CPX-2662; DNA-directed RNA polymerase II complex.
DR DIP; DIP-611N; -.
DR IntAct; P04050; 57.
DR MINT; P04050; -.
DR STRING; 4932.YDL140C; -.
DR CarbonylDB; P04050; -.
DR iPTMnet; P04050; -.
DR MaxQB; P04050; -.
DR PaxDb; P04050; -.
DR PRIDE; P04050; -.
DR TopDownProteomics; P04050; -.
DR EnsemblFungi; YDL140C_mRNA; YDL140C; YDL140C.
DR GeneID; 851415; -.
DR KEGG; sce:YDL140C; -.
DR SGD; S000002299; RPO21.
DR VEuPathDB; FungiDB:YDL140C; -.
DR eggNOG; KOG0260; Eukaryota.
DR GeneTree; ENSGT00930000151033; -.
DR HOGENOM; CLU_000487_3_0_1; -.
DR InParanoid; P04050; -.
DR OMA; SLLHICM; -.
DR BioCyc; YEAST:G3O-29539-MON; -.
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-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; P04050; -.
DR PRO; PR:P04050; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P04050; protein.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0019985; P:translesion synthesis; IMP:SGD.
DR DisProt; DP02527; -.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 3.30.1360.140; -; 1.
DR Gene3D; 4.10.860.120; -; 2.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
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; IPR042102; RNA_pol_Rpb1_3_sf.
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 InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
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;
KW 3D-structure; DNA-binding; DNA-directed RNA polymerase; Isopeptide bond;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transferase; Ubl conjugation;
KW Zinc.
FT CHAIN 1..1733
FT /note="DNA-directed RNA polymerase II subunit RPB1"
FT /id="PRO_0000073946"
FT REPEAT 1549..1555
FT /note="1"
FT REPEAT 1556..1562
FT /note="2"
FT REPEAT 1563..1569
FT /note="3"
FT REPEAT 1570..1576
FT /note="4"
FT REPEAT 1577..1583
FT /note="5"
FT REPEAT 1584..1590
FT /note="6"
FT REPEAT 1591..1597
FT /note="7"
FT REPEAT 1598..1604
FT /note="8"
FT REPEAT 1605..1611
FT /note="9"
FT REPEAT 1612..1618
FT /note="10"
FT REPEAT 1619..1625
FT /note="11"
FT REPEAT 1626..1632
FT /note="12"
FT REPEAT 1633..1639
FT /note="13"
FT REPEAT 1640..1646
FT /note="14"
FT REPEAT 1647..1653
FT /note="15"
FT REPEAT 1654..1660
FT /note="16"
FT REPEAT 1661..1667
FT /note="17"
FT REPEAT 1668..1674
FT /note="18"
FT REPEAT 1675..1681
FT /note="19"
FT REPEAT 1682..1688
FT /note="20"
FT REPEAT 1689..1695
FT /note="21"
FT REPEAT 1696..1702
FT /note="22"
FT REPEAT 1703..1709
FT /note="23"
FT REPEAT 1710..1716
FT /note="24; approximate"
FT REGION 248..260
FT /note="Lid loop"
FT REGION 306..323
FT /note="Rudder loop"
FT REGION 810..822
FT /note="Bridging helix"
FT REGION 1537..1733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1549..1716
FT /note="C-terminal domain (CTD); 24 X 7 AA approximate
FT tandem repeats of Y-S-P-T-S-P-[A-S-N-G]"
FT COMPBIAS 1537..1720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23151482,
FT ECO:0000269|PubMed:25652824, ECO:0007744|PDB:4BBR,
FT ECO:0007744|PDB:4V1M"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23151482,
FT ECO:0000269|PubMed:25652824, ECO:0007744|PDB:4BBR,
FT ECO:0007744|PDB:4V1M"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23151482,
FT ECO:0000269|PubMed:25652824, ECO:0007744|PDB:4BBR,
FT ECO:0007744|PDB:4V1M"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23151482,
FT ECO:0000269|PubMed:25652824, ECO:0007744|PDB:4BBR,
FT ECO:0007744|PDB:4V1M"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23151482,
FT ECO:0000269|PubMed:25652824, ECO:0007744|PDB:4BBR,
FT ECO:0007744|PDB:4V1M"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23151482,
FT ECO:0000269|PubMed:25652824, ECO:0007744|PDB:4BBR,
FT ECO:0007744|PDB:4V1M"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23151482,
FT ECO:0000269|PubMed:25652824, ECO:0007744|PDB:4BBR,
FT ECO:0007744|PDB:4V1M"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23151482,
FT ECO:0000269|PubMed:25652824, ECO:0007744|PDB:4BBR,
FT ECO:0007744|PDB:4V1M"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:23151482,
FT ECO:0000269|PubMed:25652824, ECO:0007744|PDB:4BBR,
FT ECO:0007744|PDB:4V1M"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared with RPB2"
FT /evidence="ECO:0000269|PubMed:23151482,
FT ECO:0000269|PubMed:25652824, ECO:0007744|PDB:4BBR,
FT ECO:0007744|PDB:4V1M"
FT BINDING 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:23151482,
FT ECO:0000269|PubMed:25652824, ECO:0007744|PDB:4BBR,
FT ECO:0007744|PDB:4V1M"
FT BINDING 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared with RPB2"
FT /evidence="ECO:0000269|PubMed:23151482,
FT ECO:0000269|PubMed:25652824, ECO:0007744|PDB:4BBR,
FT ECO:0007744|PDB:4V1M"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:23151482,
FT ECO:0000269|PubMed:25652824, ECO:0007744|PDB:4BBR,
FT ECO:0007744|PDB:4V1M"
FT MOD_RES 1471
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 695
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 1246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 1350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT VARIANT 1653..1659
FT /note="Missing (in strain: A364A)"
FT CONFLICT 1514
FT /note="A -> V (in Ref. 1; CAA26904)"
FT /evidence="ECO:0000305"
FT CONFLICT 1524
FT /note="G -> A (in Ref. 1; CAA26904)"
FT /evidence="ECO:0000305"
FT CONFLICT 1601
FT /note="T -> M (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2NVT"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3S14"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3CQZ"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1I50"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1I50"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2NVQ"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2E2I"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:6O6C"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:1I50"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1I50"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:3S2H"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:4BBR"
FT HELIX 261..280
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:3CQZ"
FT HELIX 286..304
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:3S14"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:3S14"
FT HELIX 325..329
FT /evidence="ECO:0007829|PDB:1I50"
FT TURN 330..335
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:6UPZ"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:7RIW"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 402..406
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:3S14"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:3CQZ"
FT TURN 419..422
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 452..454
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 455..470
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 495..504
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 507..510
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 514..517
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 525..535
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:3S1N"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 543..552
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 553..555
FT /evidence="ECO:0007829|PDB:3CQZ"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 574..581
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:2E2I"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:3PO2"
FT STRAND 604..608
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 611..615
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 619..622
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:1I50"
FT HELIX 629..637
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 639..658
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 666..669
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 673..699
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 706..708
FT /evidence="ECO:0007829|PDB:1I50"
FT HELIX 710..736
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 742..749
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 750..752
FT /evidence="ECO:0007829|PDB:1K83"
FT HELIX 755..762
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 773..775
FT /evidence="ECO:0007829|PDB:7RIQ"
FT STRAND 779..781
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 782..784
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 794..798
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 804..806
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 810..845
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 849..851
FT /evidence="ECO:0007829|PDB:7NKX"
FT TURN 852..854
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 855..857
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 863..867
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 868..870
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 875..877
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 878..882
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 884..886
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 890..897
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 901..903
FT /evidence="ECO:0007829|PDB:2YU9"
FT TURN 904..906
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 910..912
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 913..915
FT /evidence="ECO:0007829|PDB:3S15"
FT HELIX 916..919
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 923..946
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 947..949
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 953..958
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 960..970
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 975..977
FT /evidence="ECO:0007829|PDB:1K83"
FT HELIX 983..994
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1005..1013
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1016..1025
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1028..1033
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1039..1056
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1064..1076
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1079..1082
FT /evidence="ECO:0007829|PDB:3S1Q"
FT HELIX 1086..1088
FT /evidence="ECO:0007829|PDB:2NVQ"
FT STRAND 1089..1091
FT /evidence="ECO:0007829|PDB:3CQZ"
FT STRAND 1092..1094
FT /evidence="ECO:0007829|PDB:3S1Q"
FT HELIX 1097..1104
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 1105..1107
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1115..1120
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1122..1126
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1128..1138
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1143..1145
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1147..1154
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1158..1160
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1164..1166
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1167..1171
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1172..1174
FT /evidence="ECO:0007829|PDB:1I50"
FT STRAND 1179..1182
FT /evidence="ECO:0007829|PDB:4BY7"
FT STRAND 1190..1197
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1199..1204
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1209..1220
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1221..1223
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1224..1228
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1233..1235
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1237..1242
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 1245..1250
FT /evidence="ECO:0007829|PDB:7RIQ"
FT TURN 1252..1255
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 1258..1270
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1272..1275
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1282..1292
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1296..1310
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1313..1316
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1317..1319
FT /evidence="ECO:0007829|PDB:6UPZ"
FT TURN 1324..1326
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1328..1330
FT /evidence="ECO:0007829|PDB:1I50"
FT HELIX 1332..1339
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1341..1357
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 1358..1360
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1365..1374
FT /evidence="ECO:0007829|PDB:1TWF"
FT TURN 1375..1377
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1378..1380
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1384..1386
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1388..1390
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1392..1394
FT /evidence="ECO:0007829|PDB:3S14"
FT HELIX 1396..1399
FT /evidence="ECO:0007829|PDB:3S14"
FT TURN 1400..1402
FT /evidence="ECO:0007829|PDB:3S14"
FT HELIX 1406..1415
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1424..1429
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1437..1439
FT /evidence="ECO:0007829|PDB:1TWF"
FT STRAND 1440..1445
FT /evidence="ECO:0007829|PDB:1TWF"
FT HELIX 1447..1453
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 1458..1460
FT /evidence="ECO:0007829|PDB:6O6C"
FT HELIX 1463..1466
FT /evidence="ECO:0007829|PDB:6O6C"
FT HELIX 1474..1476
FT /evidence="ECO:0007829|PDB:5VKO"
FT STRAND 1677..1680
FT /evidence="ECO:0007829|PDB:2LO6"
FT STRAND 1689..1691
FT /evidence="ECO:0007829|PDB:5M9D"
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
