TOP2_TRYCR
ID TOP2_TRYCR Reviewed; 1232 AA.
AC P30190;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 119.
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 Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1331785; DOI=10.1016/0166-6851(92)90133-5;
RA Fragoso S.P., Goldenberg S.;
RT "Cloning and characterization of the gene encoding Trypanosoma cruzi DNA
RT topoisomerase II.";
RL Mol. Biochem. Parasitol. 55:127-134(1992).
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 -!- 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; M91165; AAA85575.1; -; Genomic_DNA.
DR PIR; A48446; A48446.
DR AlphaFoldDB; P30190; -.
DR SMR; P30190; -.
DR VEuPathDB; TriTrypDB:BCY84_02073; -.
DR VEuPathDB; TriTrypDB:C3747_112g72; -.
DR VEuPathDB; TriTrypDB:C4B63_26g233; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_5797; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_5798; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0119150; -.
DR VEuPathDB; TriTrypDB:TcCL_ESM04813; -.
DR VEuPathDB; TriTrypDB:TcCLB.506445.60; -.
DR VEuPathDB; TriTrypDB:TcCLB.508277.370; -.
DR VEuPathDB; TriTrypDB:TCDM_03128; -.
DR VEuPathDB; TriTrypDB:TcG_04548; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_007048; -.
DR VEuPathDB; TriTrypDB:TcYC6_0012170; -.
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..1232
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145379"
FT DOMAIN 432..546
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 952..961
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1161..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 771
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 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 122..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 135..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 352..354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 438
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 515
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 515
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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 SITE 466
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 469
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 636
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 637
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 689
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 729
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 770
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 822
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1232 AA; 138440 MW; A0C53933E6FC6B77 CRC64;
MAEASKYKKL TPIDHVLIRP EMYVGSVDTS SSSMFVFDHE KGRMVWESLK VNHGLLKIVD
EILLNASDNI ANKGGRMTYI RVHITEAGEI TIENDGAGIP IVRSKEHKLY IPEMVFGHLL
TSSNYDDTSQ NAVAGRHGYG AKLTNILSHR FSVCCRTKGK EFHMSWHDHM RRATAPRVSN
VDPKEKNLTR VKFLPDYERF GLDANKISHD MKRVLHKRIM DLAAMFPSIE ISLNGVPFAF
KSFADYAMLY SSPSSSGEMP PAPFVYESRN GAIAFIPSLT AGTRRIFGVV NGVVTHNGGT
HCNAAQEVLQ SSLESVEKAL KKDNKVIDTN RVLRHFMILV FLVQVQPKFD SQNKARLVSV
PTMPRVPRQE LMDFLLRMPF LEAHVNTVTG QLADELNKEM GAGRRMSSKS LISSITKLVD
ATTTRRDPRF VRTLIVTEGD SAKALAQNSL SSDQKRYTGV FPLRGKLLNV RNKNLKRLKN
CKELQELFCA LGLELGKIYK DAEELRYQRL LVMTDQDADG SHIKGLVINA FEALWPSLLN
RNPGFISIFS TPIVKVRLRD KSTHSFFSLK EFHKWQKTHG NVSYTAKYYK ALGTSTTAEG
KEYFKDMDKH TMRLVVERND HKLLDSVFDS QEVEWRKDWM TKANAYTGEV DIDRSKKTLT
VPDFVHKEMV HFALAGNARA LAHAVDGLKP SQRKILWAIM RRSGNESAKV AQLSGYISEV
SAFHHGEMSL QETIIKMAQN FTGGNNINLL IPEGQFGSRQ QLGNDHAAAR YIFTKLSSLA
RILFPSEDEP LLDYVTEEGQ QVEPNHYVPI LPLLLCNGSV GIGFGFASNI PPFHPLDVSA
AVRSMINGEA AKVVVRRLVP WAVGYQGEVR RGPEGEFIAA GSYQYYVDGR VHVTEIPWTL
SIEAFRDHIS VLASKDVVQR IADYSGANHV DIDLELTNGA MTTYAECESE LSLTQRIYIN
GTVFSPTGVL TPLEGDLAPV LQWHYDRRLD LYKKRRQRNL GLLEAELARE KSTLKFVTHF
REGKIDIVNA TDDSLAKTCS KLGMVRVDDS YDYVLRKPIT FYTKTSLENL NRKISETEKR
IDKLKKTAPV QMWLDELDRF DRAFEEHENT AVATILKERR VNPPTGDVSR NLQQPRLELE
EVKVSSSGGK SVPMRVRVRK YVPPPPSKRP HVGQSVGGGG GGGSVRSSAA AVVAHVKAEK
KAARARSMQK MLLDVVARQV ARVLPRLPWF LF
