TOP2_ARATH
ID TOP2_ARATH Reviewed; 1473 AA.
AC P30182; Q38807;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=DNA topoisomerase 2;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE AltName: Full=DNA topoisomerase II;
GN Name=TOP2; OrderedLocusNames=At3g23890; ORFNames=F14O13.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=7846176; DOI=10.1104/pp.106.4.1701;
RA Xie S., Lam E.;
RT "Characterization of a DNA Topoisomerase II cDNA from Arabidopsis
RT thaliana.";
RL Plant Physiol. 106:1701-1702(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1202-1304.
RC STRAIN=cv. Columbia, and cv. Kas-1;
RX PubMed=7838729; DOI=10.1093/nar/22.25.5729;
RA Xie S., Lam E.;
RT "Abundance of nuclear DNA topoisomerase II is correlated with proliferation
RT in Arabidopsis thaliana.";
RL Nucleic Acids Res. 22:5729-5736(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 751-838.
RA Gerhold D., Parsons A., Hadwiger L.A.;
RT "PCR-assisted cloning of a topoisomerase II gene from Arabidopsis.";
RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
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.
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
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};
CC -!- SUBUNIT: Homodimer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P30182-1; Sequence=Displayed;
CC -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC negative and positive supercoils, whereas prokaryotic enzymes relax
CC only negative supercoils.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
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DR EMBL; L21015; AAA65448.1; -; mRNA.
DR EMBL; AP001297; BAB03006.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76826.1; -; Genomic_DNA.
DR EMBL; U12284; AAC48999.1; -; Genomic_DNA.
DR EMBL; U12285; AAC49000.1; -; Genomic_DNA.
DR EMBL; M84654; AAA32877.1; -; Genomic_DNA.
DR PIR; S53598; S53599.
DR RefSeq; NP_189031.1; NM_113294.3. [P30182-1]
DR AlphaFoldDB; P30182; -.
DR SMR; P30182; -.
DR STRING; 3702.AT3G23890.1; -.
DR iPTMnet; P30182; -.
DR PaxDb; P30182; -.
DR PRIDE; P30182; -.
DR ProteomicsDB; 232464; -. [P30182-1]
DR EnsemblPlants; AT3G23890.1; AT3G23890.1; AT3G23890. [P30182-1]
DR GeneID; 821972; -.
DR Gramene; AT3G23890.1; AT3G23890.1; AT3G23890. [P30182-1]
DR KEGG; ath:AT3G23890; -.
DR Araport; AT3G23890; -.
DR TAIR; locus:2076201; AT3G23890.
DR eggNOG; KOG0355; Eukaryota.
DR InParanoid; P30182; -.
DR PhylomeDB; P30182; -.
DR PRO; PR:P30182; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P30182; baseline and differential.
DR Genevisible; P30182; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003916; F:DNA topoisomerase activity; ISS:TAIR.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0000819; P:sister chromatid segregation; IBA:GO_Central.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; DNA-binding; Isomerase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..1473
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145380"
FT DOMAIN 455..569
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..347
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 980..989
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1195..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1457..1473
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 794
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 148..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 161..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 378..380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 461
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 BINDING 538
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 BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 489
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 492
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 662
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 663
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 712
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 746
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 752
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 793
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 845
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
FT SITE 924
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT VARIANT 1213
FT /note="K -> N (in strain: cv. Kas-1)"
FT VARIANT 1245
FT /note="A -> G (in strain: cv. Kas-1)"
FT VARIANT 1299
FT /note="E -> G (in strain: cv. Kas-1)"
SQ SEQUENCE 1473 AA; 164107 MW; 00B6C4836E381403 CRC64;
MATKLPLQNS NAANVAKAPA KSRAAAGGKT IEEMYQKKSQ LEHILLRPDT YIGSIEKHTQ
TLWVYEKDEM VQRPVTYVPG LYKIFDEILV NAADNKQRDA KMDSVQVVID VEQNLISVCN
SGAGVPVEIH QEEGIYVPEM IFGHLLTSSN YDDNVKKTTG GRNGYGAKLT NIFSTEFIIE
TADGKRLKKY KQVFENNMGK KSEPVITKCN KSENWTKVTF KPDLKKFNMT ELEDDVVALM
SKRVFDIAGC LGKSVKVELN GKQIPVKSFT DYVDLYLSAA NKSRTEDPLP RLTEKVNDRW
EVCVSLSEGQ FQQVSFVNSI ATIKGGTHVD YVTSQITNHI VAAVNKKNKN ANVKAHNVKN
HLWVFVNALI DNPAFDSQTK ETLTLRQSSF GSKCELSEDF LKKVGKSGVV ENLLSWADFK
QNKDLKKSDG AKTGRVLVEK LDDAAEAGGK NSRLCTLILT EGDSAKSLAL AGRSVLGNNY
CGVFPLRGKL LNVREASTTQ ITNNKEIENL KKILGLKQNM KYENVNSLRY GQMMIMTDQD
HDGSHIKGLL INFIHSFWPS LLQVPSFLVE FITPIVKATR KGTKKVLSFY SMPEYEEWKE
SLKGNATGWD IKYYKGLGTS TAEEGKEYFS NLGLHKKDFV WEDEQDGEAI ELAFSKKKIE
ARKNWLSSYV PGNHLDQRQP KVTYSDFVNK ELILFSMADL QRSIPSMVDG LKPGQRKILF
VAFKKIARKE MKVAQLVGYV SLLSAYHHGE QSLASAIIGM AQDYVGSNNI NLLLPNGQFG
TRTSGGKDSA SARYIFTKLS PVTRILFPKD DDLLLDYLNE DGQRIEPTWY MPIIPTVLVN
GAEGIGTGWS TFIPNYNPRE IVANVRRLLN GESMVPMDPW YRGFKGTIEK TASKEGGCTY
TITGLYEEVD ETTIRITELP IRRWNDDYKN FLQSLKTDNG APFFQDVKAY NDEKSVDFDL
ILSEENMLAA RQEGFLKKFK LTTTIATSNM HLFDKKGVIK KYVTPEQILE EFFDLRFEYY
EKRKETVVKN MEIELLKLEN KARFILAVLS GEIIVNKRKK ADIVEDLRQK GFTPFPRKAE
SVEAAIAGAV DDDAAEEPEE ILVDPESSSS YIPGSEYDYL LAMAIASLTI EKVEELLADR
DKMIIAVADM KKTTPKSLWL SDLESLDKEL EKLDLKDAQV QQAIEAAQKK IRAKSGAAVK
VKRQAPKKPA PKKTTKKASE SETTEASYSA MDTDNNVAEV VKPKARQGAK KKASESETTE
ASHSAMDTDN NVAEVVKPKG RQGAKKKAPA AAKEVEEDEM LDLAQRLAQY NFGSAPADSS
KTAETSKAIA VDDDDDDVVV EVAPVKKGGR KPAATKAAKP PAAPRKRGKQ TVASTEVLAI
GVSPEKKVRK MRSSPFNKKS SSVMSRLADN KEEESSENVA GNSSSEKSGG DVSAISRPQR
ANRRKMTYVL SDSESESAND SEFDDIEDDE DDE
