RPB2_YEAST
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 03-AUG-2022, entry version 225.
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}.
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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; 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 PDBsum; 1I3Q; -.
DR PDBsum; 1I50; -.
DR PDBsum; 1I6H; -.
DR PDBsum; 1K83; -.
DR PDBsum; 1NIK; -.
DR PDBsum; 1NT9; -.
DR PDBsum; 1PQV; -.
DR PDBsum; 1R5U; -.
DR PDBsum; 1R9S; -.
DR PDBsum; 1R9T; -.
DR PDBsum; 1SFO; -.
DR PDBsum; 1TWA; -.
DR PDBsum; 1TWC; -.
DR PDBsum; 1TWF; -.
DR PDBsum; 1TWG; -.
DR PDBsum; 1TWH; -.
DR PDBsum; 1WCM; -.
DR PDBsum; 1Y1V; -.
DR PDBsum; 1Y1W; -.
DR PDBsum; 1Y1Y; -.
DR PDBsum; 1Y77; -.
DR PDBsum; 2B63; -.
DR PDBsum; 2B8K; -.
DR PDBsum; 2E2H; -.
DR PDBsum; 2E2I; -.
DR PDBsum; 2E2J; -.
DR PDBsum; 2JA5; -.
DR PDBsum; 2JA6; -.
DR PDBsum; 2JA7; -.
DR PDBsum; 2JA8; -.
DR PDBsum; 2NVQ; -.
DR PDBsum; 2NVT; -.
DR PDBsum; 2NVX; -.
DR PDBsum; 2NVY; -.
DR PDBsum; 2NVZ; -.
DR PDBsum; 2R7Z; -.
DR PDBsum; 2R92; -.
DR PDBsum; 2R93; -.
DR PDBsum; 2VUM; -.
DR PDBsum; 2YU9; -.
DR PDBsum; 3CQZ; -.
DR PDBsum; 3FKI; -.
DR PDBsum; 3GTG; -.
DR PDBsum; 3GTJ; -.
DR PDBsum; 3GTK; -.
DR PDBsum; 3GTL; -.
DR PDBsum; 3GTM; -.
DR PDBsum; 3GTO; -.
DR PDBsum; 3GTP; -.
DR PDBsum; 3GTQ; -.
DR PDBsum; 3H3V; -.
DR PDBsum; 3HOU; -.
DR PDBsum; 3HOV; -.
DR PDBsum; 3HOW; -.
DR PDBsum; 3HOX; -.
DR PDBsum; 3HOY; -.
DR PDBsum; 3HOZ; -.
DR PDBsum; 3I4M; -.
DR PDBsum; 3I4N; -.
DR PDBsum; 3J0K; -.
DR PDBsum; 3J1N; -.
DR PDBsum; 3K1F; -.
DR PDBsum; 3K7A; -.
DR PDBsum; 3M3Y; -.
DR PDBsum; 3M4O; -.
DR PDBsum; 3PO2; -.
DR PDBsum; 3PO3; -.
DR PDBsum; 3QT1; -.
DR PDBsum; 3RZD; -.
DR PDBsum; 3RZO; -.
DR PDBsum; 3S14; -.
DR PDBsum; 3S15; -.
DR PDBsum; 3S16; -.
DR PDBsum; 3S17; -.
DR PDBsum; 3S1M; -.
DR PDBsum; 3S1N; -.
DR PDBsum; 3S1Q; -.
DR PDBsum; 3S1R; -.
DR PDBsum; 3S2D; -.
DR PDBsum; 3S2H; -.
DR PDBsum; 4A3B; -.
DR PDBsum; 4A3C; -.
DR PDBsum; 4A3D; -.
DR PDBsum; 4A3E; -.
DR PDBsum; 4A3F; -.
DR PDBsum; 4A3G; -.
DR PDBsum; 4A3I; -.
DR PDBsum; 4A3J; -.
DR PDBsum; 4A3K; -.
DR PDBsum; 4A3L; -.
DR PDBsum; 4A3M; -.
DR PDBsum; 4A93; -.
DR PDBsum; 4BBR; -.
DR PDBsum; 4BBS; -.
DR PDBsum; 4BXX; -.
DR PDBsum; 4BXZ; -.
DR PDBsum; 4BY1; -.
DR PDBsum; 4BY7; -.
DR PDBsum; 4V1M; -.
DR PDBsum; 4V1N; -.
DR PDBsum; 4V1O; -.
DR PDBsum; 4X67; -.
DR PDBsum; 4X6A; -.
DR PDBsum; 4Y52; -.
DR PDBsum; 4Y7N; -.
DR PDBsum; 5C3E; -.
DR PDBsum; 5C44; -.
DR PDBsum; 5C4A; -.
DR PDBsum; 5C4J; -.
DR PDBsum; 5C4X; -.
DR PDBsum; 5FMF; -.
DR PDBsum; 5FYW; -.
DR PDBsum; 5FZ5; -.
DR PDBsum; 5IP7; -.
DR PDBsum; 5IP9; -.
DR PDBsum; 5OQJ; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5OT2; -.
DR PDBsum; 5SVA; -.
DR PDBsum; 5U5Q; -.
DR PDBsum; 5VVR; -.
DR PDBsum; 5VVS; -.
DR PDBsum; 5W4U; -.
DR PDBsum; 5W51; -.
DR PDBsum; 6BLO; -.
DR PDBsum; 6BLP; -.
DR PDBsum; 6BM2; -.
DR PDBsum; 6BM4; -.
DR PDBsum; 6BQF; -.
DR PDBsum; 6GYK; -.
DR PDBsum; 6GYL; -.
DR PDBsum; 6GYM; -.
DR PDBsum; 6I84; -.
DR PDBsum; 6O6C; -.
DR PDBsum; 6UPX; -.
DR PDBsum; 6UPY; -.
DR PDBsum; 6UPZ; -.
DR PDBsum; 6UQ0; -.
DR PDBsum; 6UQ1; -.
DR PDBsum; 6UQ2; -.
DR PDBsum; 6UQ3; -.
DR PDBsum; 7KED; -.
DR PDBsum; 7KEE; -.
DR PDBsum; 7KEF; -.
DR PDBsum; 7NKX; -.
DR PDBsum; 7NKY; -.
DR PDBsum; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 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; P08518; -.
DR SMR; P08518; -.
DR BioGRID; 34547; 493.
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; P08518; -.
DR PRIDE; P08518; -.
DR EnsemblFungi; YOR151C_mRNA; YOR151C; YOR151C.
DR GeneID; 854322; -.
DR KEGG; sce:YOR151C; -.
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; RDLHGTH; -.
DR BioCyc; YEAST:G3O-33668-MON; -.
DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SCE-72086; mRNA Capping.
DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR EvolutionaryTrace; 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:0006366; P:transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0001172; P:transcription, RNA-templated; IEA:GOC.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 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; PTHR20856; 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 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 87..91
FT /evidence="ECO:0007829|PDB:7RIP"
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 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 886..888
FT /evidence="ECO:0007829|PDB:4BBR"
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 STRAND 924..926
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 931..933
FT /evidence="ECO:0007829|PDB:6O6C"
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
