TOP2_LEICH
ID TOP2_LEICH Reviewed; 1236 AA.
AC O61078;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 105.
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 Leishmania chagasi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=44271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MHOM/BR/86/L669;
RA Tepe-Lansdell T., Mann B.J., Labombard M., Macdonald T., Slunt K.M.,
RA Pearson R.D.;
RT "Isolation of a gene encoding a DNA topoisomerase II of Leishmania
RT (Leishmania) chagasi.";
RL Submitted (NOV-1999) 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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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; AF051307; AAC05295.2; -; Genomic_DNA.
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 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 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..1236
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145376"
FT DOMAIN 434..548
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 956..965
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1161..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 775
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 124..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 137..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 354..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 440
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 517
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 517
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 519
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 468
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 471
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 640
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 641
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 693
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 733
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 774
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 826
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1236 AA; 138970 MW; A3209B95A078045C CRC64;
MTYASKYKKL TPIDHVLLRP EMYVGSIETQ PTPMYIFDPE KGRMVWETMR VNQGLLKIVD
EILLNAADNI NNSKGSVRQT YISIHISDTG EITVENDGAG LPIVRSREHK MYIPEMVFGH
LLTSSNYNND STSTTAGRHG YGAKLTNILS TKFSVVCRTD GRESHMSWTD HMRMATAPRV
NRVDPKEKSV TRVKFMPDYA HFGFPNASIS LDMKRVLHKR IMDLAAMFSK IEVRLNNVPF
GFRTFTDYAR LYSLPGLDGS MPPEPFVYTS PNGSVAYVPQ LTQSPKRIVG VVNGVVTYNG
GTHCNAAMDI LDSCLDSLSK NFKKNGKVVD TNRVQRHFTV LVFLIQTQPK FDSQSKARLV
STVTMPRMPK NTLEKYLERM PFLEAHVNSM DDQLANELNK EIGAGRRLSS KTLISAITKL
VDATSSQPDG RNIRTLIITE GDSAKALALN SLSSEQKKYC GVFPLRGKLL NVRNKNLKRL
KTCKGLQDLF LSLGLELGKE YRSPAELRYQ RLLVMTDQDA DGSHIKGLVI NAFESLWPKL
LQNNPGYISL FSTPIVKIKV SGKSKEVIAF HSFRDFHRWQ RAHPSARYTA KYYKGLGTST
TAEGKEYFAD MEKNIMQLTV DARDHQLLDS VFDAAEVEWR KEWMTKANAF QGEVDIDRSK
KTLTIPEFVH KEMVHFALVG NARAIPHCVD GLKPSQRKIL WAMLRRHNSE ASKVAQLSGY
ISEASAFHHG EASLQETIVK MAQNFTGGNN INLLVPEGQF GSRQQLGNDH AAPRYIFTKL
SRFGRLLFPE EDDPLLDYMD EEGTFVEPHH YVPILPMLLC NGAVGIGFGF ATTIPSFHPL
DVSAAVRAMI NGESAKQVVR NLVPWAVGFQ GTVRRGPDNE FIAVGKYTAH PNGRFHISEI
PWMTSIEAFR LHISSLASAD VVQRIADYSG ANHIDIDLIV RDGSLTTWAE CETDLALAQR
IYINGTVFSP TGTLSPIDSD LSPVLQWHYD RRLDLYKRRR TRKIGLMKMD LARLQSTRKF
VEHFRQGQID FLNATDDTLH KTCVKLGLVR VDESFDYILK KPITFFTRTS TEKLQADIAK
TQAQIEELKR TTPVKMWLTE LDKFDKTFQE YERVLINSIQ KEQRSSSITG GVELPALRQP
LLMLGASAKG ATAYRVHACQ YEKPPPSKRR PGESVGGARP SDSAARTVGK RLVGSRSEFK
NKKPMSRKNN VKVSLSTRVA QXPGAQLGRL LPHVLM
