TOP2_YEAST
ID TOP2_YEAST Reviewed; 1428 AA.
AC P06786; D6W191;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 235.
DE RecName: Full=DNA topoisomerase 2;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:18097402, ECO:0000269|PubMed:23022727, ECO:0000269|PubMed:9685374};
DE AltName: Full=DNA topoisomerase II;
GN Name=TOP2; Synonyms=TOR3; OrderedLocusNames=YNL088W; ORFNames=N2244;
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].
RX PubMed=3017975; DOI=10.1016/s0021-9258(18)67108-x;
RA Giaever F., Lynn R., Goto T., Wang J.C.;
RT "The complete nucleotide sequence of the structural gene TOP2 of yeast DNA
RT topoisomerase II.";
RL J. Biol. Chem. 261:12448-12454(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S96, YJM 320, and YJM 326;
RX PubMed=11907579; DOI=10.1038/416326a;
RA Steinmetz L.M., Sinha H., Richards D.R., Spiegelman J.I., Oefner P.J.,
RA McCusker J.H., Davis R.W.;
RT "Dissecting the architecture of a quantitative trait locus in yeast.";
RL Nature 416:326-330(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8740422;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<485::aid-yea928>3.0.co;2-u;
RA Soler-Mira A., Saiz J.E., Ballesta J.P.G., Remacha M.A.;
RT "The sequence of a 17,933 bp segment of Saccharomyces cerevisiae chromosome
RT XIV contains the RHO2, TOP2, MKT1 and END3 genes and five new open reading
RT frames.";
RL Yeast 12:485-491(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
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 [6]
RP REVIEW ON PHOSPHORYLATION.
RX PubMed=1332607; DOI=10.1007/bf00584459;
RA Gasser S.M., Walter R., Dang Q., Cardenas M.E.;
RT "Topoisomerase II: its functions and phosphorylation.";
RL Antonie Van Leeuwenhoek 62:15-24(1992).
RN [7]
RP PHOSPHORYLATION AT THR-1086; SER-1087; THR-1258; SER-1266; SER-1269;
RP SER-1272; SER-1353; SER-1356; SER-1408 AND SER-1423.
RX PubMed=1316274; DOI=10.1002/j.1460-2075.1992.tb05230.x;
RA Cardenas M.E., Dang Q., Glover C.V., Gasser S.M.;
RT "Casein kinase II phosphorylates the eukaryote-specific C-terminal domain
RT of topoisomerase II in vivo.";
RL EMBO J. 11:1785-1796(1992).
RN [8]
RP SUBUNIT, ACTIVE SITE, CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF
RP ARG-690; ASP-697; LYS-700; ARG-704; HIS-736; ARG-781; TYR-782 AND ASN-828.
RX PubMed=9685374; DOI=10.1074/jbc.273.32.20252;
RA Liu Q., Wang J.C.;
RT "Identification of active site residues in the 'GyrA' half of yeast DNA
RT topoisomerase II.";
RL J. Biol. Chem. 273:20252-20260(1998).
RN [9]
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 [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1252, AND IDENTIFICATION BY
RP 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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 410-1202.
RX PubMed=8538787; DOI=10.1038/379225a0;
RA Berger J.M., Gamblin S.J., Harrison S.C., Wang J.C.;
RT "Structure and mechanism of DNA topoisomerase II.";
RL Nature 379:225-232(1996).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 409-1201.
RX PubMed=10201398; DOI=10.1038/7556;
RA Fass D., Bogden C.E., Berger J.M.;
RT "Quaternary changes in topoisomerase II may direct orthogonal movement of
RT two DNA strands.";
RL Nat. Struct. Biol. 6:322-326(1999).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-413 IN COMPLEX WITH ATP ANALOG,
RP AND SUBUNIT.
RX PubMed=12963818; DOI=10.1073/pnas.1832879100;
RA Classen S., Olland S., Berger J.M.;
RT "Structure of the topoisomerase II ATPase region and its mechanism of
RT inhibition by the chemotherapeutic agent ICRF-187.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10629-10634(2003).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 419-1177 IN COMPLEX WITH DNA AND
RP MAGNESIUM, CATALYTIC ACTIVITY, COFACTOR, AND SITE.
RX PubMed=18097402; DOI=10.1038/nature06396;
RA Dong K.C., Berger J.M.;
RT "Structural basis for gate-DNA recognition and bending by type IIA
RT topoisomerases.";
RL Nature 450:1201-1205(2007).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 421-1177 IN COMPLEX WITH DNA AND
RP ZINC IONS, ACTIVE SITE, ENZYME MECHANISM, COFACTOR, AND SITE.
RX PubMed=20485342; DOI=10.1038/nature08974;
RA Schmidt B.H., Burgin A.B., Deweese J.E., Osheroff N., Berger J.M.;
RT "A novel and unified two-metal mechanism for DNA cleavage by type II and IA
RT topoisomerases.";
RL Nature 465:641-644(2010).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (4.4 ANGSTROMS) OF 1-1177 IN COMPLEX WITH DNA AND ATP
RP ANALOG, CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
RX PubMed=23022727; DOI=10.1038/nsmb.2388;
RA Schmidt B.H., Osheroff N., Berger J.M.;
RT "Structure of a topoisomerase II-DNA-nucleotide complex reveals a new
RT control mechanism for ATPase activity.";
RL Nat. Struct. Mol. Biol. 19:1147-1154(2012).
CC -!- FUNCTION: Control of topological states of DNA by transient breakage
CC and subsequent rejoining of DNA strands. Topoisomerase II makes double-
CC strand breaks. Essential during mitosis and meiosis for proper
CC segregation of daughter chromosomes. {ECO:0000269|PubMed:23022727,
CC ECO:0000269|PubMed:9685374}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00995, ECO:0000269|PubMed:18097402,
CC ECO:0000269|PubMed:23022727, ECO:0000269|PubMed:9685374};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995,
CC ECO:0000269|PubMed:18097402, ECO:0000269|PubMed:20485342};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995,
CC ECO:0000269|PubMed:18097402, ECO:0000269|PubMed:20485342};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995,
CC ECO:0000269|PubMed:18097402, ECO:0000269|PubMed:20485342};
CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges
CC with both the protein and the DNA. Can also accept other divalent metal
CC cations, such as Mn(2+) or Ca(2+). {ECO:0000255|PROSITE-
CC ProRule:PRU00995, ECO:0000269|PubMed:18097402,
CC ECO:0000269|PubMed:20485342};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12963818,
CC ECO:0000269|PubMed:18097402, ECO:0000269|PubMed:20485342,
CC ECO:0000269|PubMed:23022727, ECO:0000269|PubMed:9685374}.
CC -!- INTERACTION:
CC P06786; P24583: PKC1; NbExp=2; IntAct=EBI-19352, EBI-9860;
CC P06786; P06786: TOP2; NbExp=5; IntAct=EBI-19352, EBI-19352;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylation enhances the activity. Stimulates decatenation
CC activity. {ECO:0000269|PubMed:1316274}.
CC -!- MISCELLANEOUS: In yeast topoisomerase II can substitute topoisomerase I
CC for the relaxing activity.
CC -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC negative and positive supercoils, whereas prokaryotic enzymes relax
CC only negative supercoils.
CC -!- MISCELLANEOUS: Present with 5730 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
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DR EMBL; M13814; AAB36610.1; -; Genomic_DNA.
DR EMBL; AF458969; AAM00518.1; -; Genomic_DNA.
DR EMBL; AF458971; AAM00530.1; -; Genomic_DNA.
DR EMBL; AF458972; AAM00536.1; -; Genomic_DNA.
DR EMBL; X89016; CAA61422.1; -; Genomic_DNA.
DR EMBL; Z71364; CAA95964.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10457.1; -; Genomic_DNA.
DR PIR; S57534; ISBYT2.
DR RefSeq; NP_014311.3; NM_001182926.3.
DR PDB; 1BGW; X-ray; 2.70 A; A=409-1201.
DR PDB; 1BJT; X-ray; 2.50 A; A=409-1201.
DR PDB; 1PVG; X-ray; 1.80 A; A/B=1-413.
DR PDB; 1QZR; X-ray; 1.90 A; A/B=1-413.
DR PDB; 2RGR; X-ray; 3.00 A; A=419-1177.
DR PDB; 3L4J; X-ray; 2.48 A; A=421-1177.
DR PDB; 3L4K; X-ray; 2.98 A; A=421-1177.
DR PDB; 4GFH; X-ray; 4.41 A; A/F=1-1177.
DR PDBsum; 1BGW; -.
DR PDBsum; 1BJT; -.
DR PDBsum; 1PVG; -.
DR PDBsum; 1QZR; -.
DR PDBsum; 2RGR; -.
DR PDBsum; 3L4J; -.
DR PDBsum; 3L4K; -.
DR PDBsum; 4GFH; -.
DR AlphaFoldDB; P06786; -.
DR SMR; P06786; -.
DR BioGRID; 35735; 233.
DR DIP; DIP-2300N; -.
DR IntAct; P06786; 34.
DR MINT; P06786; -.
DR STRING; 4932.YNL088W; -.
DR BindingDB; P06786; -.
DR ChEMBL; CHEMBL5290; -.
DR iPTMnet; P06786; -.
DR MaxQB; P06786; -.
DR PaxDb; P06786; -.
DR PRIDE; P06786; -.
DR EnsemblFungi; YNL088W_mRNA; YNL088W; YNL088W.
DR GeneID; 855636; -.
DR KEGG; sce:YNL088W; -.
DR SGD; S000005032; TOP2.
DR VEuPathDB; FungiDB:YNL088W; -.
DR eggNOG; KOG0355; Eukaryota.
DR GeneTree; ENSGT00940000168342; -.
DR HOGENOM; CLU_001935_1_1_1; -.
DR InParanoid; P06786; -.
DR OMA; TWTQDFK; -.
DR BioCyc; YEAST:G3O-33117-MON; -.
DR BRENDA; 5.6.2.2; 984.
DR Reactome; R-SCE-4615885; SUMOylation of DNA replication proteins.
DR EvolutionaryTrace; P06786; -.
DR PRO; PR:P06786; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P06786; protein.
DR GO; GO:0097047; C:DNA replication termination region; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000795; C:synaptonemal complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IMP:SGD.
DR GO; GO:0031055; P:chromatin remodeling at centromere; IMP:SGD.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IMP:SGD.
DR GO; GO:0006265; P:DNA topological change; IDA:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0000019; P:regulation of mitotic recombination; IMP:SGD.
DR GO; GO:0097046; P:replication fork progression beyond termination site; IMP:SGD.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0009303; P:rRNA transcription; IGI:SGD.
DR GO; GO:0000819; P:sister chromatid segregation; IBA:GO_Central.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
DR DisProt; DP00076; -.
DR Gene3D; 1.10.268.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.90.199.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034157; TOPRIM_TopoII.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA-binding; Isomerase; Magnesium;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..1428
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145387"
FT DOMAIN 443..557
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 333..336
FT /note="Interaction with DNA"
FT /evidence="ECO:0000305|PubMed:23022727"
FT REGION 965..974
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:20485342"
FT REGION 1083..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1428
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 782
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000269|PubMed:20485342,
FT ECO:0000269|PubMed:9685374"
FT BINDING 70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12963818"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12963818"
FT BINDING 127..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12963818"
FT BINDING 140..147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12963818"
FT BINDING 365..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12963818"
FT BINDING 449
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995,
FT ECO:0000269|PubMed:18097402"
FT BINDING 526
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995,
FT ECO:0000269|PubMed:18097402"
FT BINDING 526
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995,
FT ECO:0000269|PubMed:18097402"
FT BINDING 528
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995,
FT ECO:0000269|PubMed:18097402"
FT SITE 477
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 480
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:20485342"
FT SITE 650
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:20485342"
FT SITE 651
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:20485342"
FT SITE 700
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:20485342"
FT SITE 734
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 740
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 781
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:20485342"
FT SITE 833
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000269|PubMed:18097402"
FT SITE 908
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT MOD_RES 1086
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:1316274"
FT MOD_RES 1087
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:1316274"
FT MOD_RES 1252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1258
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:1316274"
FT MOD_RES 1266
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:1316274"
FT MOD_RES 1269
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:1316274"
FT MOD_RES 1272
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:1316274"
FT MOD_RES 1353
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:1316274"
FT MOD_RES 1356
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:1316274"
FT MOD_RES 1408
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:1316274"
FT MOD_RES 1423
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:1316274"
FT MUTAGEN 333..336
FT /note="KKKK->AAAA: Reduced enzyme activity; abolishes
FT stimulation of ATPase activity upon DNA binding."
FT MUTAGEN 333..336
FT /note="KKKK->AEEA: Strongly reduced enzyme activity;
FT abolishes stimulation of ATPase activity upon DNA binding."
FT MUTAGEN 690
FT /note="R->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:9685374"
FT MUTAGEN 697
FT /note="D->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:9685374"
FT MUTAGEN 700
FT /note="K->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:9685374"
FT MUTAGEN 704
FT /note="R->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:9685374"
FT MUTAGEN 736
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:9685374"
FT MUTAGEN 781
FT /note="R->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:9685374"
FT MUTAGEN 782
FT /note="Y->F: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:9685374"
FT MUTAGEN 828
FT /note="N->A: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:9685374"
FT CONFLICT 74
FT /note="N -> NN (in Ref. 1; AAB36610)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="P -> L (in Ref. 1; AAB36610)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="W -> R (in Ref. 1; AAB36610)"
FT /evidence="ECO:0000305"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1PVG"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:1PVG"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:1PVG"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:1PVG"
FT HELIX 58..77
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:1PVG"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:1PVG"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1PVG"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1PVG"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:1PVG"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:1PVG"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:1PVG"
FT HELIX 203..206
FT /evidence="ECO:0007829|PDB:1PVG"
FT HELIX 213..229
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1PVG"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:1PVG"
FT TURN 253..257
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:1PVG"
FT HELIX 315..332
FT /evidence="ECO:0007829|PDB:1PVG"
FT HELIX 342..346
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:1PVG"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:1PVG"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:1PVG"
FT HELIX 385..391
FT /evidence="ECO:0007829|PDB:1PVG"
FT HELIX 395..405
FT /evidence="ECO:0007829|PDB:1PVG"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 438..442
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 444..450
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 451..464
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 466..475
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:1BGW"
FT HELIX 486..491
FT /evidence="ECO:0007829|PDB:2RGR"
FT HELIX 492..502
FT /evidence="ECO:0007829|PDB:1BJT"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:1BGW"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 513..517
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 519..525
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 527..530
FT /evidence="ECO:0007829|PDB:1BGW"
FT HELIX 534..545
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 547..550
FT /evidence="ECO:0007829|PDB:1BGW"
FT STRAND 555..558
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 563..568
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 574..580
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 581..590
FT /evidence="ECO:0007829|PDB:1BJT"
FT TURN 591..594
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 609..629
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 634..642
FT /evidence="ECO:0007829|PDB:2RGR"
FT HELIX 647..656
FT /evidence="ECO:0007829|PDB:2RGR"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:2RGR"
FT HELIX 678..691
FT /evidence="ECO:0007829|PDB:1BJT"
FT TURN 695..697
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 701..713
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 721..732
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 736..738
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 741..749
FT /evidence="ECO:0007829|PDB:1BJT"
FT TURN 753..755
FT /evidence="ECO:0007829|PDB:2RGR"
FT STRAND 760..765
FT /evidence="ECO:0007829|PDB:1BJT"
FT TURN 770..773
FT /evidence="ECO:0007829|PDB:1BJT"
FT TURN 780..782
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 784..787
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 791..794
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 797..802
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 805..808
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 811..816
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 824..827
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 830..833
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 838..841
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 846..857
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 874..880
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 883..887
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 889..894
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 897..902
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 909..920
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 924..926
FT /evidence="ECO:0007829|PDB:1BGW"
FT STRAND 932..935
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 938..940
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 943..946
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 949..958
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 960..963
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 967..971
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 975..978
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 984..989
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 990..1034
FT /evidence="ECO:0007829|PDB:1BJT"
FT STRAND 1041..1043
FT /evidence="ECO:0007829|PDB:1BGW"
FT HELIX 1045..1054
FT /evidence="ECO:0007829|PDB:1BJT"
FT TURN 1108..1110
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 1114..1117
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 1121..1124
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 1126..1147
FT /evidence="ECO:0007829|PDB:1BJT"
FT HELIX 1151..1176
FT /evidence="ECO:0007829|PDB:1BJT"
SQ SEQUENCE 1428 AA; 164215 MW; 0E29EB8B89AA1387 CRC64;
MSTEPVSASD KYQKISQLEH ILKRPDTYIG SVETQEQLQW IYDEETDCMI EKNVTIVPGL
FKIFDEILVN AADNKVRDPS MKRIDVNIHA EEHTIEVKND GKGIPIEIHN KENIYIPEMI
FGHLLTSSNY DDDEKKVTGG RNGYGAKLCN IFSTEFILET ADLNVGQKYV QKWENNMSIC
HPPKITSYKK GPSYTKVTFK PDLTRFGMKE LDNDILGVMR RRVYDINGSV RDINVYLNGK
SLKIRNFKNY VELYLKSLEK KRQLDNGEDG AAKSDIPTIL YERINNRWEV AFAVSDISFQ
QISFVNSIAT TMGGTHVNYI TDQIVKKISE ILKKKKKKSV KSFQIKNNMF IFINCLIENP
AFTSQTKEQL TTRVKDFGSR CEIPLEYINK IMKTDLATRM FEIADANEEN ALKKSDGTRK
SRITNYPKLE DANKAGTKEG YKCTLVLTEG DSALSLAVAG LAVVGRDYYG CYPLRGKMLN
VREASADQIL KNAEIQAIKK IMGLQHRKKY EDTKSLRYGH LMIMTDQDHD GSHIKGLIIN
FLESSFPGLL DIQGFLLEFI TPIIKVSITK PTKNTIAFYN MPDYEKWREE ESHKFTWKQK
YYKGLGTSLA QEVREYFSNL DRHLKIFHSL QGNDKDYIDL AFSKKKADDR KEWLRQYEPG
TVLDPTLKEI PISDFINKEL ILFSLADNIR SIPNVLDGFK PGQRKVLYGC FKKNLKSELK
VAQLAPYVSE CTAYHHGEQS LAQTIIGLAQ NFVGSNNIYL LLPNGAFGTR ATGGKDAAAA
RYIYTELNKL TRKIFHPADD PLYKYIQEDE KTVEPEWYLP ILPMILVNGA EGIGTGWSTY
IPPFNPLEII KNIRHLMNDE ELEQMHPWFR GWTGTIEEIE PLRYRMYGRI EQIGDNVLEI
TELPARTWTS TIKEYLLLGL SGNDKIKPWI KDMEEQHDDN IKFIITLSPE EMAKTRKIGF
YERFKLISPI SLMNMVAFDP HGKIKKYNSV NEILSEFYYV RLEYYQKRKD HMSERLQWEV
EKYSFQVKFI KMIIEKELTV TNKPRNAIIQ ELENLGFPRF NKEGKPYYGS PNDEIAEQIN
DVKGATSDEE DEESSHEDTE NVINGPEELY GTYEYLLGMR IWSLTKERYQ KLLKQKQEKE
TELENLLKLS AKDIWNTDLK AFEVGYQEFL QRDAEARGGN VPNKGSKTKG KGKRKLVDDE
DYDPSKKNKK STARKGKKIK LEDKNFERIL LEQKLVTKSK APTKIKKEKT PSVSETKTEE
EENAPSSTSS SSIFDIKKED KDEGELSKIS NKFKKISTIF DKMGSTSATS KENTPEQDDV
ATKKNQTTAK KTAVKPKLAK KPVRKQQKVV ELSGESDLEI LDSYTDREDS NKDEDDAIPQ
RSRRQRSSRA ASVPKKSYVE TLELSDDSFI EDDEEENQGS DVSFNEED
