TOP2_CANAX
ID TOP2_CANAX Reviewed; 1461 AA.
AC P87078;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hannington 2402E;
RX PubMed=9164874; DOI=10.1042/bj3240329;
RA Keller B.A., Patel S., Fisher L.M.;
RT "Molecular cloning and expression of the Candida albicans TOP2 gene allows
RT study of fungal DNA topoisomerase II inhibitors in yeast.";
RL Biochem. J. 324:329-339(1997).
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; Y10377; CAA71405.1; -; Genomic_DNA.
DR AlphaFoldDB; P87078; -.
DR SMR; P87078; -.
DR PRIDE; P87078; -.
DR VEuPathDB; FungiDB:C4_06600W_A; -.
DR VEuPathDB; FungiDB:CAWG_03168; -.
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 GO; GO:0061982; P:meiosis I cell cycle process; IEA:UniProt.
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; 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; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Topoisomerase.
FT CHAIN 1..1461
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145382"
FT DOMAIN 498..614
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..389
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT REGION 1024..1033
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT REGION 1122..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1150
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1461
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 842
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 177..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 190..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 418..420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 504
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 583
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 583
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 585
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 532
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 535
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 710
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 711
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 760
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 794
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 800
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 841
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 893
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
FT SITE 968
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
SQ SEQUENCE 1461 AA; 165387 MW; B2F7933B05804E36 CRC64;
MSESESDYFT DGSEDDFVPT SKKSTKKNAS SKSKQPLGDA TNSTVSSSRS STPKPTNASE
TYQKLSQLEH ILKRPDTYIG SVEKTKTEMW CFDAETESMV FKEVTIVPGL YKIFDEILVN
AADNKIRDPS MKNIRVKIDA ENNIIEVMND GKGIPIEMHT KENMYIPELI FGNLLTSSNY
DDDQKKVTGG RNGFGAKLCN IFSTQFEVET ADLNMGKLYK QSWTNNMSNV SKPKITTLRT
KKEYTKITFR PDLSKFDMDC LDNDLLSVLR RRVYDLCGTV KNCNIYLNDK RLNISSFKGY
VEMYVKAIKE RSPEPEPQDG TIKNFTTIVH EVFNDRWEVA FAVSDGSFNQ VSFVNSIATT
SGGTHVKYVS DQIINKLVET LSKKEKGKKK LMIKPQEVRD NMFLFINCLI ENPAFTSQTK
EQLTTKVSQF GGKDKFVAND NLINRILKTS IVDKIRAIAN ANEDKALQKA DGSRKSRIKG
QVNLVDANKA GTKDGHNCTL ILTEGLSAMN LAVAGLSVVG RDYYGCFPLR GKLLNVREAS
ADQISKNAEI NSLKQIIGLQ HKKVYTAENI KSLRYGHIMI MTDQDQDGSH IKGLIINFLE
TSFPGLLDIP GFLLEFITPI VKVTVKARGA GGKRVIPFYT MPEFEHWRDT EGKQCRWTQK
YYKGLGTSTP MEAREYFTAL DRHLKRFHAL QGEDKDYIDL AFSKKKADER KEWLQGFLPG
THLDPEITEI PISDFINKEF ILFSMSDNVR SIPSVLDGFK PGQRKVLYGC FKKKLRSEIK
VAQLAGYVSE NTGYHHGEQS LVQTIIGLAQ NFVGSNNINV LKPNGSFGSR AAGGKDFSAA
RYIFTELSEI TRKIFNPLDD PLYTYVQDDE QTVEPEWYLP VLPMILVNGA EGIGTGWSTN
IPSYNPKDLV TNIRRLMNGE ELQEMTPWYK GWGGDLEPMG PQKFKVSGRI EQIDSNTVEI
TEIPVKTWTN NVKEFLLSGF GNEKTQPWIK DMEEHHTTSI RFVVKLTDAE MQKSLRIGLL
ERFKLVSSLS LANMVAFDPM GRIKKYNDVL EIIKDFYYVR LEYYQKRKDY MTDNLQNQLL
MLSEQARFIK MIIEKQLSVA NKKKKQLVAL LEEHNFTKFS KDGKPIKSSE ELLTGDDADE
EEETQEQEGD EDVGNTSVAN IQEGEPEQAA HVPETIYSSY DYLLGMAIWS LTYERFMRIM
QQRDQKEAEL NALLSKSAKD LWNQDLDEFL AEFDKFLLRD EQERESLASN GKKKSTKRRA
KATATKDQPN NKKVKVEPKE KKSTSAKPIV KKEASNEPQA SSSSKPKEKD DILSFFSSSS
SSAKKTTKPS GRATSNKEIE TITLFSDDDD DEDIFNLNSS SSTKVKKEAK SRSATPAAEK
SKKSKSSGKQ SILDELEDLE ILGNFDKPEP KERRTRETAS TTKRNTKKKP VIIDSDDEDE
DEEDDIVMSD GDDDDDFIVD E
