ID RPB2_YEAST Reviewed; 1224 AA. AC P08518; D6W2K8; Q12738; Q7Z9Y0; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 27-MAR-2024, entry version 234. DE RecName: Full=DNA-directed RNA polymerase II subunit RPB2; DE Short=RNA polymerase II subunit 2; DE EC=2.7.7.6; DE AltName: Full=B150; DE AltName: Full=DNA-directed RNA polymerase II 140 kDa polypeptide; GN Name=RPB2; Synonyms=RPB150, RPO22; OrderedLocusNames=YOR151C; 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 204508 / S288c; RX PubMed=3547406; DOI=10.1073/pnas.84.5.1192; RA Sweetser D., Nonet M., Young R.A.; RT "Prokaryotic and eukaryotic RNA polymerases have homologous core RT subunits."; RL Proc. Natl. Acad. Sci. U.S.A. 84:1192-1196(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=S288c / FY1678; RX PubMed=9046089; RX DOI=10.1002/(sici)1097-0061(199701)13:1<73::aid-yea52>3.0.co;2-m; RA Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B., RA Martin R.P.; RT "Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae RT chromosome XV."; RL Yeast 13:73-83(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169874; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(1997). RN [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 549-773. RC STRAIN=ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632; RX PubMed=12748053; DOI=10.1016/s1567-1356(03)00012-6; RA Kurtzman C.P., Robnett C.J.; RT "Phylogenetic relationships among yeasts of the 'Saccharomyces complex' RT determined from multigene sequence analyses."; RL FEMS Yeast Res. 3:417-432(2003). RN [6] RP PROTEIN SEQUENCE OF 837-844. RX PubMed=2204624; DOI=10.1016/s0021-9258(17)46250-8; RA Riva M., Carles C., Sentenac A., Grachev M.A., Mustaev A.A., RA Zaychikov E.F.; RT "Mapping the active site of yeast RNA polymerase B (II)."; RL J. Biol. Chem. 265:16498-16503(1990). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-919, AND IDENTIFICATION BY RP 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-919, 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 [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [10] RP ELECTRON MICROSCOPY OF THE RNA POL II/TFIIF COMPLEX. RX PubMed=14580350; DOI=10.1016/s1097-2765(03)00387-3; RA Chung W.H., Craighead J.L., Chang W.H., Ezeokonkwo C., Bareket-Samish A., RA Kornberg R.D., Asturias F.J.; RT "RNA polymerase II/TFIIF structure and conserved organization of the RT initiation complex."; RL Mol. Cell 12:1003-1013(2003). RN [11] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [12] 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 [13] 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 [14] 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 [15] 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 [16] 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 [17] 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 [18] 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 [19] 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] RP X-RAY CRYSTALLOGRAPHY (4.15 ANGSTROMS) OF THE RNA POL II COMPLEX. RX PubMed=16765890; DOI=10.1016/j.str.2006.04.003; RA Meyer P.A., Ye P., Zhang M., Suh M.H., Fu J.; RT "Phasing RNA polymerase II using intrinsically bound Zn atoms: an updated RT structural model."; RL Structure 14:973-982(2006). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC Second largest component of RNA polymerases II which synthesizes mRNA CC precursors and many functional non-coding RNAs. Proposed to contribute CC to the polymerase catalytic activity and forms the polymerase active CC center together with the largest subunit. Pol II is the central CC component of the basal RNA polymerase II transcription machinery. CC During a transcription cycle, Pol II, general transcription factors and CC the Mediator complex assemble as the preinitiation complex (PIC) at the CC promoter. 11-15 base pairs of DNA surrounding the transcription start CC site are melted and the single-stranded DNA template strand of the CC promoter is positioned deeply within the central active site cleft of CC Pol II to form the open complex. After synthesis of about 30 bases of CC RNA, Pol II releases its contacts with the core promoter and the rest CC of the transcription machinery (promoter clearance) and enters the CC stage of transcription elongation in which it moves on the template as CC the transcript elongates. Pol II appears to oscillate between inactive CC and active conformations at each step of nucleotide addition. Pol II is CC composed of mobile elements that move relative to each other. The core CC element with the central large cleft comprises RPB3, RBP10, RPB11, CC RPB12 and 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. The cleft is surrounded by jaws: an upper jaw formed by portions CC of RBP1, RPB2 and RPB9, and a lower jaw. The jaws are thought to grab CC the incoming DNA template. The fork loop 1 (RPB2) interacts with the CC RNA-DNA hybrid, possibly stabilizing it. 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. {ECO:0000269|PubMed:11805306, CC ECO:0000269|PubMed:12914699, ECO:0000269|PubMed:16341226}. CC -!- INTERACTION: CC P08518; P22139: RPB10; NbExp=2; IntAct=EBI-15767, EBI-15802; CC P08518; P16370: RPB3; NbExp=5; IntAct=EBI-15767, EBI-15773; CC P08518; P20434: RPB5; NbExp=25; IntAct=EBI-15767, EBI-15781; CC P08518; P07703: RPC40; NbExp=2; IntAct=EBI-15767, EBI-15831; CC P08518; P04050: RPO21; NbExp=4; IntAct=EBI-15767, EBI-15760; CC P08518; P41896: TFG2; NbExp=7; IntAct=EBI-15767, EBI-18916; CC -!- SUBCELLULAR LOCATION: Nucleus. 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 coordinated by three conserved aspartate CC residues of the two largest RNA Pol II subunits. CC -!- MISCELLANEOUS: Present with 18700 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M15693; AAA68096.1; -; Genomic_DNA. DR EMBL; U55020; AAC49637.1; -; Genomic_DNA. DR EMBL; Z75059; CAA99357.1; -; Genomic_DNA. DR EMBL; AF527884; AAP57849.1; -; Genomic_DNA. DR EMBL; BK006948; DAA10924.1; -; Genomic_DNA. DR PIR; A25884; A25884. DR RefSeq; NP_014794.3; NM_001183570.3. DR PDB; 1I3Q; X-ray; 3.10 A; B=1-1224. DR PDB; 1I50; X-ray; 2.80 A; B=1-1224. DR PDB; 1I6H; X-ray; 3.30 A; B=1-1224. DR PDB; 1K83; X-ray; 2.80 A; B=1-1224. DR PDB; 1NIK; X-ray; 4.10 A; B=1-1224. DR PDB; 1NT9; X-ray; 4.20 A; B=1-1224. DR PDB; 1PQV; X-ray; 3.80 A; B=1-1224. DR PDB; 1R5U; X-ray; 4.50 A; B=1-1224. DR PDB; 1R9S; X-ray; 4.25 A; B=1-1224. DR PDB; 1R9T; X-ray; 3.50 A; B=1-1224. DR PDB; 1SFO; X-ray; 3.61 A; B=1-1224. DR PDB; 1TWA; X-ray; 3.20 A; B=1-1224. DR PDB; 1TWC; X-ray; 3.00 A; B=1-1224. DR PDB; 1TWF; X-ray; 2.30 A; B=1-1224. DR PDB; 1TWG; X-ray; 3.30 A; B=1-1224. DR PDB; 1TWH; X-ray; 3.40 A; B=1-1224. DR PDB; 1WCM; X-ray; 3.80 A; B=1-1224. DR PDB; 1Y1V; X-ray; 3.80 A; B=1-1224. DR PDB; 1Y1W; X-ray; 4.00 A; B=1-1224. DR PDB; 1Y1Y; X-ray; 4.00 A; B=1-1224. DR PDB; 1Y77; X-ray; 4.50 A; B=1-1224. DR PDB; 2B63; X-ray; 3.80 A; B=1-1224. DR PDB; 2B8K; X-ray; 4.15 A; B=1-1224. DR PDB; 2E2H; X-ray; 3.95 A; B=1-1224. DR PDB; 2E2I; X-ray; 3.41 A; B=1-1224. DR PDB; 2E2J; X-ray; 3.50 A; B=1-1224. DR PDB; 2JA5; X-ray; 3.80 A; B=1-1224. DR PDB; 2JA6; X-ray; 4.00 A; B=1-1224. DR PDB; 2JA7; X-ray; 3.80 A; B/N=1-1224. DR PDB; 2JA8; X-ray; 3.80 A; B=1-1224. DR PDB; 2NVQ; X-ray; 2.90 A; B=1-1224. DR PDB; 2NVT; X-ray; 3.36 A; B=1-1224. DR PDB; 2NVX; X-ray; 3.60 A; B=1-1224. DR PDB; 2NVY; X-ray; 3.40 A; B=1-1224. DR PDB; 2NVZ; X-ray; 4.30 A; B=1-1224. DR PDB; 2R7Z; X-ray; 3.80 A; B=1-1224. DR PDB; 2R92; X-ray; 3.80 A; B=1-1224. DR PDB; 2R93; X-ray; 4.00 A; B=1-1224. DR PDB; 2VUM; X-ray; 3.40 A; B=1-1224. DR PDB; 2YU9; X-ray; 3.40 A; B=1-1224. DR PDB; 3CQZ; X-ray; 2.80 A; B=1-1223. DR PDB; 3FKI; X-ray; 3.88 A; B=1-1224. DR PDB; 3GTG; X-ray; 3.78 A; B=1-1224. DR PDB; 3GTJ; X-ray; 3.42 A; B=1-1224. DR PDB; 3GTK; X-ray; 3.80 A; B=1-1224. DR PDB; 3GTL; X-ray; 3.38 A; B=1-1224. DR PDB; 3GTM; X-ray; 3.80 A; B=1-1224. DR PDB; 3GTO; X-ray; 4.00 A; B=1-1224. DR PDB; 3GTP; X-ray; 3.90 A; B=1-1224. DR PDB; 3GTQ; X-ray; 3.80 A; B=1-1224. DR PDB; 3H3V; X-ray; 4.00 A; C=1-1224. DR PDB; 3HOU; X-ray; 3.20 A; B/N=1-1224. DR PDB; 3HOV; X-ray; 3.50 A; B=1-1224. DR PDB; 3HOW; X-ray; 3.60 A; B=1-1224. DR PDB; 3HOX; X-ray; 3.65 A; B=1-1224. DR PDB; 3HOY; X-ray; 3.40 A; B=1-1224. DR PDB; 3HOZ; X-ray; 3.65 A; B=1-1224. DR PDB; 3I4M; X-ray; 3.70 A; B=1-1224. DR PDB; 3I4N; X-ray; 3.90 A; B=1-1224. DR PDB; 3J0K; EM; 36.00 A; B=1-1224. DR PDB; 3J1N; EM; 16.00 A; B=1-1224. DR PDB; 3K1F; X-ray; 4.30 A; B=1-1224. DR PDB; 3K7A; X-ray; 3.80 A; B=1-1224. DR PDB; 3M3Y; X-ray; 3.18 A; B=1-1224. DR PDB; 3M4O; X-ray; 3.57 A; B=1-1224. DR PDB; 3PO2; X-ray; 3.30 A; B=1-1224. DR PDB; 3PO3; X-ray; 3.30 A; B=1-1224. DR PDB; 3QT1; X-ray; 4.30 A; B=1-1224. DR PDB; 3RZD; X-ray; 3.30 A; B=1-1224. DR PDB; 3RZO; X-ray; 3.00 A; B=1-1224. DR PDB; 3S14; X-ray; 2.85 A; B=1-1224. DR PDB; 3S15; X-ray; 3.30 A; B=1-1224. DR PDB; 3S16; X-ray; 3.24 A; B=1-1224. DR PDB; 3S17; X-ray; 3.20 A; B=1-1224. DR PDB; 3S1M; X-ray; 3.13 A; B=1-1224. DR PDB; 3S1N; X-ray; 3.10 A; B=1-1224. DR PDB; 3S1Q; X-ray; 3.30 A; B=1-1224. DR PDB; 3S1R; X-ray; 3.20 A; B=1-1224. DR PDB; 3S2D; X-ray; 3.20 A; B=1-1224. DR PDB; 3S2H; X-ray; 3.30 A; B=1-1224. DR PDB; 4A3B; X-ray; 3.50 A; B=1-1224. DR PDB; 4A3C; X-ray; 3.50 A; B=1-1224. DR PDB; 4A3D; X-ray; 3.40 A; B=1-1224. DR PDB; 4A3E; X-ray; 3.40 A; B=1-1224. DR PDB; 4A3F; X-ray; 3.50 A; B=1-1224. DR PDB; 4A3G; X-ray; 3.50 A; B=1-1224. DR PDB; 4A3I; X-ray; 3.80 A; B=1-1224. DR PDB; 4A3J; X-ray; 3.70 A; B=1-1224. DR PDB; 4A3K; X-ray; 3.50 A; B=1-1224. DR PDB; 4A3L; X-ray; 3.50 A; B=1-1224. DR PDB; 4A3M; X-ray; 3.90 A; B=1-1224. DR PDB; 4A93; X-ray; 3.40 A; B=1-1224. DR PDB; 4BBR; X-ray; 3.40 A; B=1-1224. DR PDB; 4BBS; X-ray; 3.60 A; B=1-1224. DR PDB; 4BXX; X-ray; 3.28 A; B=1-1224. DR PDB; 4BXZ; X-ray; 4.80 A; B=1-1224. DR PDB; 4BY1; X-ray; 3.60 A; B=1-1224. DR PDB; 4BY7; X-ray; 3.15 A; B=1-1224. DR PDB; 4V1M; EM; 6.60 A; B=1-1224. DR PDB; 4V1N; EM; 7.80 A; B=1-1224. DR PDB; 4V1O; EM; 9.70 A; B=1-1224. DR PDB; 4X67; X-ray; 4.10 A; B=1-1224. DR PDB; 4X6A; X-ray; 3.96 A; B=1-1224. DR PDB; 4Y52; X-ray; 3.50 A; B=1-1224. DR PDB; 4Y7N; X-ray; 3.30 A; B=1-1224. DR PDB; 5C3E; X-ray; 3.70 A; B=1-1224. DR PDB; 5C44; X-ray; 3.95 A; B=1-1224. DR PDB; 5C4A; X-ray; 4.20 A; B=1-1224. DR PDB; 5C4J; X-ray; 4.00 A; B=1-1224. DR PDB; 5C4X; X-ray; 4.00 A; B=1-1224. DR PDB; 5FMF; EM; 6.00 A; B=1-1224. DR PDB; 5FYW; EM; 4.35 A; B=1-1224. DR PDB; 5FZ5; EM; 8.80 A; B=1-1224. DR PDB; 5IP7; X-ray; 3.52 A; B=2-1224. DR PDB; 5IP9; X-ray; 3.90 A; B=2-1224. DR PDB; 5OQJ; EM; 4.70 A; B=1-1224. DR PDB; 5OQM; EM; 5.80 A; B=1-1224. DR PDB; 5OT2; X-ray; 3.20 A; B=1-1224. DR PDB; 5SVA; EM; 15.30 A; B=1-1224. DR PDB; 5U5Q; X-ray; 3.80 A; B=1-1224. DR PDB; 5VVR; EM; 5.80 A; B=1-1224. DR PDB; 5VVS; EM; 6.40 A; B=1-1224. DR PDB; 5W4U; X-ray; 3.60 A; B=1-1224. DR PDB; 5W51; X-ray; 3.40 A; B=1-1224. DR PDB; 6BLO; X-ray; 3.40 A; B=1-1224. DR PDB; 6BLP; X-ray; 3.20 A; B=1-1224. DR PDB; 6BM2; X-ray; 3.40 A; B=1-1224. DR PDB; 6BM4; X-ray; 2.95 A; B=1-1224. DR PDB; 6BQF; X-ray; 3.35 A; B=1-1224. DR PDB; 6GYK; EM; 5.10 A; B=1-1224. DR PDB; 6GYL; EM; 4.80 A; B=1-1224. DR PDB; 6GYM; EM; 6.70 A; B=1-1224. DR PDB; 6I84; EM; 4.40 A; B=1-1224. DR PDB; 6O6C; EM; 3.10 A; B=1-1224. DR PDB; 6UPX; X-ray; 3.40 A; B=1-1224. DR PDB; 6UPY; X-ray; 3.40 A; B=1-1224. DR PDB; 6UPZ; X-ray; 3.10 A; B=1-1224. DR PDB; 6UQ0; X-ray; 3.56 A; B=1-1224. DR PDB; 6UQ1; X-ray; 3.60 A; B=1-1224. DR PDB; 6UQ2; X-ray; 3.20 A; B=1-1224. DR PDB; 6UQ3; X-ray; 3.47 A; B=1-1224. DR PDB; 7KED; X-ray; 3.60 A; B=1-1224. DR PDB; 7KEE; X-ray; 3.45 A; B=1-1224. DR PDB; 7KEF; X-ray; 3.89 A; B=1-1224. DR PDB; 7MEI; EM; 3.54 A; B/b=1-1224. DR PDB; 7MK9; EM; 3.54 A; B=1-1224. DR PDB; 7MKA; EM; 3.54 A; b=1-1224. DR PDB; 7ML0; EM; 3.00 A; B=1-1224. DR PDB; 7ML1; EM; 4.00 A; B=1-1224. DR PDB; 7ML2; EM; 3.40 A; B=1-1224. DR PDB; 7ML4; EM; 3.10 A; B=1-1224. DR PDB; 7NKX; EM; 2.90 A; B=1-1224. DR PDB; 7NKY; EM; 3.20 A; B=1-1224. DR PDB; 7O4I; EM; 3.20 A; B=1-1224. DR PDB; 7O4J; EM; 2.90 A; B=1-1224. DR PDB; 7O4K; EM; 3.60 A; B=1-1224. DR PDB; 7O4L; EM; 3.40 A; B=1-1224. DR PDB; 7O72; EM; 3.40 A; B=1-1224. DR PDB; 7O73; EM; 3.40 A; B=1-1224. DR PDB; 7O75; EM; 3.20 A; B=1-1224. DR PDB; 7RIM; X-ray; 2.90 A; B=1-1224. DR PDB; 7RIP; X-ray; 3.30 A; B=1-1224. DR PDB; 7RIQ; X-ray; 3.00 A; B=1-1224. DR PDB; 7RIW; X-ray; 3.20 A; B=1-1224. DR PDB; 7RIX; X-ray; 3.40 A; B=1-1224. DR PDB; 7RIY; X-ray; 3.70 A; B=1-1224. DR PDB; 7UI9; EM; 3.30 A; B=1-1224. DR PDB; 7UIF; EM; 4.60 A; B=1-1224. DR PDB; 7UIO; EM; 3.30 A; AB/BB=1-1224. DR PDB; 7ZS9; EM; 3.10 A; B=1-1224. DR PDB; 7ZSA; EM; 4.00 A; B=1-1224. DR PDB; 7ZSB; EM; 6.60 A; B=1-1224. DR PDB; 8CEN; EM; 3.00 A; B=1-1224. DR PDB; 8CEO; EM; 3.60 A; B=1-1224. DR PDBsum; 1I3Q; -. DR PDBsum; 1I50; -. DR PDBsum; 1I6H; -. DR PDBsum; 1K83; -. DR PDBsum; 1NIK; -. DR PDBsum; 1NT9; -. DR PDBsum; 1PQV; -. DR PDBsum; 1R5U; -. DR PDBsum; 1R9S; -. DR PDBsum; 1R9T; -. DR PDBsum; 1SFO; -. DR PDBsum; 1TWA; -. DR PDBsum; 1TWC; -. DR PDBsum; 1TWF; -. DR PDBsum; 1TWG; -. DR PDBsum; 1TWH; -. DR PDBsum; 1WCM; -. DR PDBsum; 1Y1V; -. DR PDBsum; 1Y1W; -. DR PDBsum; 1Y1Y; -. DR PDBsum; 1Y77; -. DR PDBsum; 2B63; -. DR PDBsum; 2B8K; -. DR PDBsum; 2E2H; -. DR PDBsum; 2E2I; -. DR PDBsum; 2E2J; -. DR PDBsum; 2JA5; -. DR PDBsum; 2JA6; -. DR PDBsum; 2JA7; -. DR PDBsum; 2JA8; -. DR PDBsum; 2NVQ; -. DR PDBsum; 2NVT; -. DR PDBsum; 2NVX; -. DR PDBsum; 2NVY; -. DR PDBsum; 2NVZ; -. DR PDBsum; 2R7Z; -. DR PDBsum; 2R92; -. DR PDBsum; 2R93; -. DR PDBsum; 2VUM; -. DR PDBsum; 2YU9; -. DR PDBsum; 3CQZ; -. DR PDBsum; 3FKI; -. DR PDBsum; 3GTG; -. DR PDBsum; 3GTJ; -. DR PDBsum; 3GTK; -. DR PDBsum; 3GTL; -. DR PDBsum; 3GTM; -. DR PDBsum; 3GTO; -. DR PDBsum; 3GTP; -. DR PDBsum; 3GTQ; -. DR PDBsum; 3H3V; -. DR PDBsum; 3HOU; -. DR PDBsum; 3HOV; -. DR PDBsum; 3HOW; -. DR PDBsum; 3HOX; -. DR PDBsum; 3HOY; -. DR PDBsum; 3HOZ; -. DR PDBsum; 3I4M; -. DR PDBsum; 3I4N; -. DR PDBsum; 3J0K; -. DR PDBsum; 3J1N; -. DR PDBsum; 3K1F; -. DR PDBsum; 3K7A; -. DR PDBsum; 3M3Y; -. DR PDBsum; 3M4O; -. DR PDBsum; 3PO2; -. DR PDBsum; 3PO3; -. DR PDBsum; 3QT1; -. DR PDBsum; 3RZD; -. DR PDBsum; 3RZO; -. DR PDBsum; 3S14; -. DR PDBsum; 3S15; -. DR PDBsum; 3S16; -. DR PDBsum; 3S17; -. DR PDBsum; 3S1M; -. DR PDBsum; 3S1N; -. DR PDBsum; 3S1Q; -. DR PDBsum; 3S1R; -. DR PDBsum; 3S2D; -. DR PDBsum; 3S2H; -. DR PDBsum; 4A3B; -. DR PDBsum; 4A3C; -. DR PDBsum; 4A3D; -. DR PDBsum; 4A3E; -. DR PDBsum; 4A3F; -. DR PDBsum; 4A3G; -. DR PDBsum; 4A3I; -. DR PDBsum; 4A3J; -. DR PDBsum; 4A3K; -. DR PDBsum; 4A3L; -. DR PDBsum; 4A3M; -. DR PDBsum; 4A93; -. DR PDBsum; 4BBR; -. DR PDBsum; 4BBS; -. DR PDBsum; 4BXX; -. DR PDBsum; 4BXZ; -. DR PDBsum; 4BY1; -. DR PDBsum; 4BY7; -. DR PDBsum; 4V1M; -. DR PDBsum; 4V1N; -. DR PDBsum; 4V1O; -. DR PDBsum; 4X67; -. DR PDBsum; 4X6A; -. DR PDBsum; 4Y52; -. DR PDBsum; 4Y7N; -. DR PDBsum; 5C3E; -. DR PDBsum; 5C44; -. DR PDBsum; 5C4A; -. DR PDBsum; 5C4J; -. DR PDBsum; 5C4X; -. DR PDBsum; 5FMF; -. DR PDBsum; 5FYW; -. DR PDBsum; 5FZ5; -. DR PDBsum; 5IP7; -. DR PDBsum; 5IP9; -. DR PDBsum; 5OQJ; -. DR PDBsum; 5OQM; -. DR PDBsum; 5OT2; -. DR PDBsum; 5SVA; -. DR PDBsum; 5U5Q; -. DR PDBsum; 5VVR; -. DR PDBsum; 5VVS; -. DR PDBsum; 5W4U; -. DR PDBsum; 5W51; -. DR PDBsum; 6BLO; -. DR PDBsum; 6BLP; -. DR PDBsum; 6BM2; -. DR PDBsum; 6BM4; -. DR PDBsum; 6BQF; -. DR PDBsum; 6GYK; -. DR PDBsum; 6GYL; -. DR PDBsum; 6GYM; -. DR PDBsum; 6I84; -. DR PDBsum; 6O6C; -. DR PDBsum; 6UPX; -. DR PDBsum; 6UPY; -. DR PDBsum; 6UPZ; -. DR PDBsum; 6UQ0; -. DR PDBsum; 6UQ1; -. DR PDBsum; 6UQ2; -. DR PDBsum; 6UQ3; -. DR PDBsum; 7KED; -. DR PDBsum; 7KEE; -. DR PDBsum; 7KEF; -. DR PDBsum; 7MEI; -. DR PDBsum; 7MK9; -. DR PDBsum; 7MKA; -. DR PDBsum; 7ML0; -. DR PDBsum; 7ML1; -. DR PDBsum; 7ML2; -. DR PDBsum; 7ML4; -. 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 PDBsum; 7UI9; -. DR PDBsum; 7UIF; -. DR PDBsum; 7UIO; -. DR PDBsum; 7ZS9; -. DR PDBsum; 7ZSA; -. DR PDBsum; 7ZSB; -. DR PDBsum; 8CEN; -. DR PDBsum; 8CEO; -. DR AlphaFoldDB; P08518; -. DR EMDB; EMD-0090; -. DR EMDB; EMD-0091; -. DR EMDB; EMD-0092; -. DR EMDB; EMD-0633; -. DR EMDB; EMD-12449; -. DR EMDB; EMD-12450; -. DR EMDB; EMD-12719; -. DR EMDB; EMD-12720; -. DR EMDB; EMD-12721; -. DR EMDB; EMD-12722; -. DR EMDB; EMD-12743; -. DR EMDB; EMD-12744; -. DR EMDB; EMD-12745; -. DR EMDB; EMD-14927; -. DR EMDB; EMD-14928; -. DR EMDB; EMD-14929; -. DR EMDB; EMD-26542; -. DR EMDB; EMD-26544; -. DR EMDB; EMD-26551; -. DR EMDB; EMD-2784; -. DR EMDB; EMD-2785; -. DR EMDB; EMD-2786; -. DR EMDB; EMD-3846; -. DR EMDB; EMD-3850; -. DR EMDB; EMD-4429; -. DR EMDB; EMD-8305; -. DR EMDB; EMD-8735; -. DR EMDB; EMD-8737; -. DR SMR; P08518; -. DR BioGRID; 34547; 507. DR ComplexPortal; CPX-2662; DNA-directed RNA polymerase II complex. DR DIP; DIP-14N; -. DR IntAct; P08518; 95. DR MINT; P08518; -. DR STRING; 4932.YOR151C; -. DR iPTMnet; P08518; -. DR MaxQB; P08518; -. DR PaxDb; 4932-YOR151C; -. DR PeptideAtlas; P08518; -. DR EnsemblFungi; YOR151C_mRNA; YOR151C; YOR151C. DR GeneID; 854322; -. DR KEGG; sce:YOR151C; -. DR AGR; SGD:S000005677; -. DR SGD; S000005677; RPB2. DR VEuPathDB; FungiDB:YOR151C; -. DR eggNOG; KOG0214; Eukaryota. DR GeneTree; ENSGT00950000183132; -. DR HOGENOM; CLU_000524_5_1_1; -. DR InParanoid; P08518; -. DR OMA; CYDRNDS; -. DR OrthoDB; 5476750at2759; -. DR BioCyc; YEAST:G3O-33668-MONOMER; -. 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-72203; Processing of Capped Intron-Containing Pre-mRNA. 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 Reactome; R-SCE-9018519; Estrogen-dependent gene expression. DR BioGRID-ORCS; 854322; 3 hits in 10 CRISPR screens. DR EvolutionaryTrace; P08518; -. DR PRO; PR:P08518; -. DR Proteomes; UP000002311; Chromosome XV. DR RNAct; P08518; 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; HDA:SGD. 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:0003729; F:mRNA binding; HDA:SGD. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0001172; P:RNA-templated transcription; IEA:GOC. DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:SGD. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:ComplexPortal. DR CDD; cd00653; RNA_pol_B_RPB2; 1. DR Gene3D; 2.40.50.150; -; 1. DR Gene3D; 3.90.1070.20; -; 1. DR Gene3D; 3.90.1100.10; -; 1. DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1. DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1. DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 1. DR InterPro; IPR015712; DNA-dir_RNA_pol_su2. DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom. DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf. DR InterPro; IPR007121; RNA_pol_bsu_CS. DR InterPro; IPR007644; RNA_pol_bsu_protrusion. DR InterPro; IPR007642; RNA_pol_Rpb2_2. DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR InterPro; IPR007646; RNA_pol_Rpb2_4. DR InterPro; IPR007647; RNA_pol_Rpb2_5. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold. DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1. DR PANTHER; PTHR20856:SF7; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2; 1. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04561; RNA_pol_Rpb2_2; 1. DR Pfam; PF04565; RNA_pol_Rpb2_3; 1. DR Pfam; PF04566; RNA_pol_Rpb2_4; 1. DR Pfam; PF04567; RNA_pol_Rpb2_5; 1. DR Pfam; PF00562; RNA_pol_Rpb2_6; 1. DR Pfam; PF04560; RNA_pol_Rpb2_7; 1. DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; DNA-directed RNA polymerase; KW Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transferase; Zinc; Zinc-finger. FT CHAIN 1..1224 FT /note="DNA-directed RNA polymerase II subunit RPB2" FT /id="PRO_0000048091" FT ZN_FING 1163..1185 FT /note="C4-type" FT REGION 467..478 FT /note="Fork loop 1" FT BINDING 837 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with RPB1" FT BINDING 1163 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 1166 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 1182 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 1185 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT MOD_RES 919 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956" FT CONFLICT 1003..1006 FT /note="AEGI -> RRRY (in Ref. 1; AAA68096)" FT /evidence="ECO:0000305" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:6BM4" FT HELIX 29..41 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:1I6H" FT HELIX 45..56 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 58..64 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 69..73 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:3GTJ" FT STRAND 81..83 FT /evidence="ECO:0007829|PDB:6O6C" FT STRAND 86..90 FT /evidence="ECO:0007829|PDB:7ML0" FT STRAND 96..102 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:3S14" FT HELIX 114..119 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 125..129 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 134..137 FT /evidence="ECO:0007829|PDB:7ML0" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:2E2I" FT HELIX 145..148 FT /evidence="ECO:0007829|PDB:6O6C" FT STRAND 150..156 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 157..160 FT /evidence="ECO:0007829|PDB:6O6C" FT STRAND 166..171 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 176..179 FT /evidence="ECO:0007829|PDB:1I3Q" FT HELIX 180..182 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 186..191 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 202..205 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 208..212 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 214..218 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 224..227 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 232..241 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 253..260 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 264..266 FT /evidence="ECO:0007829|PDB:1K83" FT STRAND 269..272 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 277..281 FT /evidence="ECO:0007829|PDB:2NVQ" FT HELIX 282..288 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 294..301 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 308..320 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 321..323 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 327..336 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:4BY7" FT HELIX 342..344 FT /evidence="ECO:0007829|PDB:3GTJ" FT HELIX 345..358 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 359..361 FT /evidence="ECO:0007829|PDB:1TWA" FT TURN 362..364 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 367..369 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 371..389 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 390..393 FT /evidence="ECO:0007829|PDB:3PO3" FT HELIX 401..403 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 404..407 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 409..433 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 435..437 FT /evidence="ECO:0007829|PDB:7RIQ" FT HELIX 438..440 FT /evidence="ECO:0007829|PDB:6O6C" FT HELIX 444..447 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 451..463 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 467..469 FT /evidence="ECO:0007829|PDB:3S14" FT TURN 471..473 FT /evidence="ECO:0007829|PDB:6UPZ" FT HELIX 474..476 FT /evidence="ECO:0007829|PDB:3S14" FT STRAND 477..479 FT /evidence="ECO:0007829|PDB:3PO3" FT STRAND 480..482 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 488..495 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 497..499 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 504..506 FT /evidence="ECO:0007829|PDB:7NKX" FT TURN 510..512 FT /evidence="ECO:0007829|PDB:7NKX" FT HELIX 516..518 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 519..521 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 530..532 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 533..535 FT /evidence="ECO:0007829|PDB:1K83" FT STRAND 536..539 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 544..547 FT /evidence="ECO:0007829|PDB:7RIM" FT HELIX 552..560 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 563..565 FT /evidence="ECO:0007829|PDB:3CQZ" FT HELIX 566..568 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 571..573 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 574..576 FT /evidence="ECO:0007829|PDB:4BY7" FT STRAND 578..582 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 585..591 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 593..606 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 607..609 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 614..618 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 619..622 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 623..627 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 633..641 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 646..649 FT /evidence="ECO:0007829|PDB:1I50" FT STRAND 650..652 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 655..666 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 681..686 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 689..694 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 695..698 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 703..706 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 707..710 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 711..713 FT /evidence="ECO:0007829|PDB:5OT2" FT STRAND 725..727 FT /evidence="ECO:0007829|PDB:6BM4" FT STRAND 739..741 FT /evidence="ECO:0007829|PDB:3S14" FT HELIX 745..748 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 753..755 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 756..758 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 759..761 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 764..773 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 774..776 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 779..781 FT /evidence="ECO:0007829|PDB:2YU9" FT TURN 783..787 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 791..798 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 803..805 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 809..812 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 813..816 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 821..827 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 829..832 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 833..837 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 838..842 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 843..847 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 848..851 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 853..861 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 867..869 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 873..875 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 880..882 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 887..889 FT /evidence="ECO:0007829|PDB:7ML0" FT HELIX 890..892 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 895..899 FT /evidence="ECO:0007829|PDB:3HOU" FT STRAND 904..906 FT /evidence="ECO:0007829|PDB:3CQZ" FT STRAND 910..912 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 914..916 FT /evidence="ECO:0007829|PDB:1K83" FT HELIX 920..923 FT /evidence="ECO:0007829|PDB:7ML2" FT STRAND 924..926 FT /evidence="ECO:0007829|PDB:7O4J" FT HELIX 928..931 FT /evidence="ECO:0007829|PDB:7ML0" FT STRAND 935..940 FT /evidence="ECO:0007829|PDB:1I50" FT STRAND 947..956 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 958..960 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 962..972 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 979..981 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 983..985 FT /evidence="ECO:0007829|PDB:1I50" FT STRAND 987..994 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 996..998 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 1001..1005 FT /evidence="ECO:0007829|PDB:5OT2" FT STRAND 1009..1012 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 1014..1016 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 1018..1021 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 1023..1038 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 1041..1043 FT /evidence="ECO:0007829|PDB:7O4J" FT STRAND 1046..1049 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 1052..1060 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 1061..1063 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 1068..1070 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 1071..1073 FT /evidence="ECO:0007829|PDB:3S1Q" FT TURN 1075..1077 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 1080..1084 FT /evidence="ECO:0007829|PDB:3S1Q" FT STRAND 1085..1097 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 1099..1101 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 1104..1106 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 1113..1115 FT /evidence="ECO:0007829|PDB:3S14" FT STRAND 1116..1118 FT /evidence="ECO:0007829|PDB:7NKX" FT HELIX 1122..1124 FT /evidence="ECO:0007829|PDB:3S14" FT STRAND 1128..1130 FT /evidence="ECO:0007829|PDB:3S14" FT HELIX 1132..1141 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 1144..1151 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 1153..1155 FT /evidence="ECO:0007829|PDB:7NKX" FT STRAND 1159..1166 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 1172..1174 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 1175..1178 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 1179..1182 FT /evidence="ECO:0007829|PDB:1TWF" FT TURN 1183..1186 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 1187..1195 FT /evidence="ECO:0007829|PDB:1TWF" FT HELIX 1198..1209 FT /evidence="ECO:0007829|PDB:1TWF" FT STRAND 1215..1218 FT /evidence="ECO:0007829|PDB:1TWF" SQ SEQUENCE 1224 AA; 138751 MW; BABD03212C0A583E CRC64; MSDLANSEKY YDEDPYGFED ESAPITAEDS WAVISAFFRE KGLVSQQLDS FNQFVDYTLQ DIICEDSTLI LEQLAQHTTE SDNISRKYEI SFGKIYVTKP MVNESDGVTH ALYPQEARLR NLTYSSGLFV DVKKRTYEAI DVPGRELKYE LIAEESEDDS ESGKVFIGRL PIMLRSKNCY LSEATESDLY KLKECPFDMG GYFIINGSEK VLIAQERSAG NIVQVFKKAA PSPISHVAEI RSALEKGSRF ISTLQVKLYG REGSSARTIK ATLPYIKQDI PIVIIFRALG IIPDGEILEH ICYDVNDWQM LEMLKPCVED GFVIQDRETA LDFIGRRGTA LGIKKEKRIQ YAKDILQKEF LPHITQLEGF ESRKAFFLGY MINRLLLCAL DRKDQDDRDH FGKKRLDLAG PLLAQLFKTL FKKLTKDIFR YMQRTVEEAH DFNMKLAINA KTITSGLKYA LATGNWGEQK KAMSSRAGVS QVLNRYTYSS TLSHLRRTNT PIGRDGKLAK PRQLHNTHWG LVCPAETPEG QACGLVKNLS LMSCISVGTD PMPIITFLSE WGMEPLEDYV PHQSPDATRV FVNGVWHGVH RNPARLMETL RTLRRKGDIN PEVSMIRDIR EKELKIFTDA GRVYRPLFIV EDDESLGHKE LKVRKGHIAK LMATEYQDIE GGFEDVEEYT WSSLLNEGLV EYIDAEEEES ILIAMQPEDL EPAEANEEND LDVDPAKRIR VSHHATTFTH CEIHPSMILG VAASIIPFPD HNQSPRNTYQ SAMGKQAMGV FLTNYNVRMD TMANILYYPQ KPLGTTRAME YLKFRELPAG QNAIVAIACY SGYNQEDSMI MNQSSIDRGL FRSLFFRSYM DQEKKYGMSI TETFEKPQRT NTLRMKHGTY DKLDDDGLIA PGVRVSGEDV IIGKTTPISP DEEELGQRTA YHSKRDASTP LRSTENGIVD QVLVTTNQDG LKFVKVRVRT TKIPQIGDKF ASRHGQKGTI GITYRREDMP FTAEGIVPDL IINPHAIPSR MTVAHLIECL LSKVAALSGN EGDASPFTDI TVEGISKLLR EHGYQSRGFE VMYNGHTGKK LMAQIFFGPT YYQRLRHMVD DKIHARARGP MQVLTRQPVE GRSRDGGLRF GEMERDCMIA HGAASFLKER LMEASDAFRV HICGICGLMT VIAKLNHNQF ECKGCDNKID IYQIHIPYAA KLLFQELMAM NITPRLYTDR SRDF //