TOP2_CRIFA
ID TOP2_CRIFA Reviewed; 1239 AA.
AC P27570;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 Crithidia fasciculata.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Crithidia.
OX NCBI_TaxID=5656;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CFC1;
RX PubMed=1311798; DOI=10.1016/0166-6851(92)90244-e;
RA Pasion S.G., Hines J.C., Aebersold R., Ray D.S.;
RT "Molecular cloning and expression of the gene encoding the kinetoplast-
RT associated type II DNA topoisomerase of Crithidia fasciculata.";
RL Mol. Biochem. Parasitol. 50:57-68(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. Mitochondrion matrix, kinetoplast.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X59623; CAA42182.1; -; Genomic_DNA.
DR PIR; A45648; A45648.
DR AlphaFoldDB; P27570; -.
DR SMR; P27570; -.
DR VEuPathDB; TriTrypDB:CFAC1_240045600; -.
DR GO; GO:0020023; C:kinetoplast; IEA:UniProtKB-SubCell.
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; Kinetoplast; Magnesium; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Nucleus; Topoisomerase.
FT CHAIN 1..1239
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145375"
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 1167..1206
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 1239 AA; 138456 MW; 9FCB801382DDBD10 CRC64;
MTDASKYQKL TPIDHVLLRP EMYVGSIETQ SIPMFVFDPA KGKMVWESMQ VNQGLLKIVD
EILLNAADNI NNSVRGARMT YISIKISDSG EIMVENDGAG LPIVKSKEHK MYIPEMVFGH
LLTSSNYNND ASSTTAGRHG YGAKLTNILS TKFSVVCRTA GREFHMSWTD HMRMATTPRV
SNVDPKEKNV TRVTFMPDYA HFGFPTAAIS LDMKRVLHKR IMDLAAMFSK IEVRLNNVPF
GFQTFNDYAR LYSLPGADGA MPPEPFVHTG PNGSIAFVPQ LTQSPKRIVG VVNGVVTYNG
GTHCTSAMEI LETGLDSLSR SLKKDGKVID TNRVARHFTV LVFLIQSQPK FDSQSKARLV
STVTMPRVPR TALDQYLAAM PFLEAHMNSM DDQLAAELNK EIGTGKRLSS RSLISSITKL
VDATSSRSDG KNIRTLIVTE GDSAKALALN SLSSEQKKFC GVFPLRGKLL NVRNKNLKRL
KTCKELQDLF LALGLELGKT YKSPAELRYQ RLLVMTDQDA DGSHIKGLVI NAFESLWPSL
LQHNPGYISL FSTPIVKIKV NGKAKEVVAF HSFRDFHRWQ RANPNARYSA KYYKGLGTST
TAEGKEYFAD MERNVMRLVV EPKDHRLLDS VFDSAEVEWR KEWMSKANAF QGEVDIDRSK
KLLTIGDFVH KEMVHFALVG NARAIPHCVD GLKPSQRKIL WAMLKRHSSE AAKVAQLSGY
ISEVSSFHHG EASLQETIVK MAQNFTGGNN INLLVPEGQF GSRQQLGNDH AAPRYIFTKL
SRFARLLFPE DDDPLLDYID EEGTMVEPNH YVPILPLLLC NGAVGIGFGF ATNIPSFHPL
DVSAAVRAMI NGESAKQVVR NLVPWAVGFQ GTVRRGPEKE YIAVGKYTAH RNGRLHVSEL
PWMTSIEAFR SHISSLASSD VVQRIADYSG ANHIDIDLIV REGSMTTWAE CETDLALSQR
IYINGTVFSP DGTLSPIDAD LSPVLQWHYD RRLDLYKRRR TRQIGLLEMD LARLQSTRKF
VEHFRQGHID FLAATDDTLT KTCVKLGLVR VDDGYDYILK KPITFYTKTS TEKLQADIKK
TQDSIAVLKQ TTPVKMWLTD LDKFDKTFQE YERVLIHSIQ KEQRPASITG GEEVPALRQP
PLMLEAPAKG AASSSYRVHI CRYEEPPASK RKPEDTYGGA LSSGGSTRNV GKRLTGARGA
KKKKVVRRTR TKMSLGTRVA EFAGAQLGRL LPQLPRLLF
