TOP2_PLAFK
ID TOP2_PLAFK Reviewed; 1398 AA.
AC P41001;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 116.
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;
OS Plasmodium falciparum (isolate K1 / Thailand).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5839;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8041616; DOI=10.1093/nar/22.13.2547;
RA Cheesman S., McAleese S., Goman M., Johnson D., Horrocks P., Ridley R.G.,
RA Kilbey B.J.;
RT "The gene encoding topoisomerase II from Plasmodium falciparum.";
RL Nucleic Acids Res. 22:2547-2551(1994).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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; X79345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P41001; -.
DR SMR; P41001; -.
DR ChEMBL; CHEMBL1741266; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 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 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; 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 3: Inferred from homology;
KW ATP-binding; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Topoisomerase.
FT CHAIN 1..1398
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145377"
FT DOMAIN 493..608
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 260..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1021
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1214..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 830
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 131..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 411..413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 499
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 577
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 577
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 579
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 527
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 530
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 697
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 698
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 747
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 781
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 788
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 829
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 881
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
FT SITE 956
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
SQ SEQUENCE 1398 AA; 161029 MW; BAAD7BEE88FE5BE9 CRC64;
MAKNKTIEER YQKKSQIEHI LLRPDTYIGS VEMHTQLLWV WNKEKNRMVQ KNITYVPGLY
KIFDEIIVNA ADVKAREKEK SENPMTCIKI EINKENKRIS VYNDGEGIPV DIHKEMNIYV
PHMIFGELLT SDNYDDAEDR ITGGRNGFGA KLTNIFSKEF IVQCGDSSRK KEFKMTWSDN
MSKFSEPHIK NYNGKDYVKV TFKPDLNKFG MTEMDDDIES LLFKRVYDLA GTCSVRVYLN
GQRLAVKDFK SYVDLYLKDN SNDNKNNKGQ NDNNNNNNNN NDENANQNND NLDVSLSNEP
ADGTPTKNNN NNNNNNDEDE IVKIHEKQHR WEIVVSKSDG SQFQQVSFVN SICTTKGGSH
VNYIVEQLLS SLSKKANAKN KGGMEIKSGH IRNHLWVFVN CLIVNPTFDS QTKETLTTKP
VKFGSKCILS DKTINNVLKS PILSNILLWA QAKAQVELKK KMKAGSSKAR ERIIGIPKLE
DANDAGSKYS QECTLILTEG DSAKTSCLAG LSIVGRDKYG VFPLKGKLLN VRDASFKQLM
DNKEIQNIFR IMGLDITDKN KDDIKGLRYG SLMIMTDQDY DGSHIKGLLI NMIHKFWPSL
LKHKGFLSEF VTPIVKVQKG SQEYSFFTIA EYEQWKENTN LLGWKIKYYK GLGTSTDREF
KQYFSDIKNH KIMFLWTGDR DGDSIDMAFS KKRIEDRKLW LQNFILGSYV DHKEKDLSYY
DFVNKELIYY SRYDTERSIP NIMDGWKPGQ RKVLYGCFKR NLRNECKVAQ LVGYIAEHSA
YHHHGESSLQ QTIINMAQTF VGSNNINFLE PCGQFGSRKE GGKDASAARY IFTKLASSTR
SIFNEYDDPI LKYLNEEGQK IEPQYYIPVI PTILVNGCEG IGTGYSSFIP NYNYKDIIDN
IKRYINKEPL IPMVPWYKDF KGRIESNGKT GYETIGIINK IDNDTLEITE LPIKKWTQDY
KEFLEELLTD EKHQLILDYI DNSSHEDICF TIKMDPAKLQ KAEEEGLEKV FKLKSTLTTT
NMTLFDPNLK LQRYSTELDI LKEFCYQRLK AYENRKSYLI SKLEKEKRII SNKTKFILAI
VNNELIVNKK KKKVLVEELY RKGYDPYKDI NKIKKEEIFE QELLDAADNP EDNEEIIAGI
TVKDYDYLLS MPIFSLTLEK VEDLLTQLKE KERELEILRN ITVETMWLKD IEKVEEAIEF
QRNVELSNRE ESNKFKVARK QGPSSMKKKK KKKKLSSDEE SEGGDTSDSS EFLVNTLNIK
KNTNKKTTTS SNNVNNSKKR LRKADDLNSN ELDNTLSVSK TFDDNNNLTD NTPLINRLND
ENNEFSSNNV DNKSTNKNSR KKKPKIADST NDNNSELNSS IQINDNVNDD INITISPNKT
INVNEFSSIK NKLLELGI
