TOP2_CANGA
ID TOP2_CANGA Reviewed; 1406 AA.
AC O93794; Q6FP95;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
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; OrderedLocusNames=CAGL0J05610g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=9782488; DOI=10.1099/00221287-144-9-2407;
RA Nakayama H., Izuta M., Nagahashi S., Sihta E.Y., Sato Y., Yamazaki T.,
RA Arisawa M., Kitada K.;
RT "A controllable gene-expression system for the pathogenic fungus Candida
RT glabrata.";
RL Microbiology 144:2407-2415(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 (By similarity). {ECO:0000250}.
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; AB010644; BAA33955.1; -; Genomic_DNA.
DR EMBL; CR380956; CAG60900.1; -; Genomic_DNA.
DR RefSeq; XP_447949.1; XM_447949.1.
DR AlphaFoldDB; O93794; -.
DR SMR; O93794; -.
DR STRING; 5478.XP_447949.1; -.
DR PRIDE; O93794; -.
DR EnsemblFungi; CAG60900; CAG60900; CAGL0J05610g.
DR GeneID; 2889445; -.
DR KEGG; cgr:CAGL0J05610g; -.
DR CGD; CAL0133128; TOP2.
DR VEuPathDB; FungiDB:CAGL0J05610g; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_1_0_1; -.
DR InParanoid; O93794; -.
DR OMA; TWTQDFK; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0034506; C:chromosome, centromeric core domain; IEA:EnsemblFungi.
DR GO; GO:0097047; C:DNA replication termination region; IEA:EnsemblFungi.
DR GO; GO:0000791; C:euchromatin; IEA:EnsemblFungi.
DR GO; GO:0000795; C:synaptonemal complex; IEA:EnsemblFungi.
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:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031055; P:chromatin remodeling at centromere; IEA:EnsemblFungi.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:EnsemblFungi.
DR GO; GO:0006265; P:DNA topological change; IEA:EnsemblFungi.
DR GO; GO:0007076; P:mitotic chromosome condensation; IEA:EnsemblFungi.
DR GO; GO:0000019; P:regulation of mitotic recombination; IEA:EnsemblFungi.
DR GO; GO:0097046; P:replication fork progression beyond termination site; IEA:EnsemblFungi.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IEA:EnsemblFungi.
DR GO; GO:0009303; P:rRNA transcription; IEA:EnsemblFungi.
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; 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; 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; Phosphoprotein; Reference proteome;
KW Topoisomerase.
FT CHAIN 1..1406
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145383"
FT DOMAIN 441..555
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 332..334
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT REGION 963..972
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT REGION 1079..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1406
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 780
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:P06786"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 126..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 139..146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 363..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 447
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 524
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 524
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 526
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 475
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 478
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 648
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 649
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 732
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 779
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 831
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
FT SITE 906
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT CONFLICT 190
FT /note="G -> V (in Ref. 1; BAA33955)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="R -> S (in Ref. 1; BAA33955)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1406 AA; 161046 MW; DFAEE38F2598E28B CRC64;
MSEPKTASER YQKISQLEHI LKRPDTYIGS VEIQEQEQWI YDEETDCMID KTVNIVPGLF
KIFDEILVNA ADNKVRDPSM KRIDVTINPE ENFIEVRNDG KGIPIEIHEK EKIYIPELIF
GHLLTSSNYD DDEKKVTGGR NGYGAKLCNI FSTEFTLETA DPKNGRKYVQ TWENNMNVCH
PPKITSYKKG PSYTKVAFKP DLSRFGMESL DSDILGVMRR RVYDINGSVR DVNVYLNGKP
LKIRNFKNYV ELYLKSLEKM RKMDNGESDT TPSNIPTILY ERVSDRWEIA FAVSDISFKQ
VSFVNSIATT TGGTHVNYIA DQIVRKVSDI LKKKKKNIKP YQIKNNMFIF INCLIENPAF
TSQTKEQLTT RVKDFGSRCD ISSDYINKIM KTDLATKIFE IADENANNAL KKSDGSRKSR
ITDYPKLEDA NKAGTKDGYK CTLILTEGDS ALSLAVAGLA VVGRDYYGCY PLRGKMLNVR
EATADQILKN AEIQAIKKIM GLQHRKKYED TKSLRYGHLM IMTDQDHDGS HIKGLIINFI
ETSFPGLLDI PGFLIEFITP IVKVTITKPI KKVISFFNLP DYEKWREEES HKYSWKQKYY
KGLGTSTSPE IIEYFSNLDT HLKKFHALQG DDKDLIDLAF SKKKADDRKE WLRQYEPGTV
LDPTLNEIPI SDFINKELIL FSLADNVRSI PSVLDGFKPG QRKVLYTCFK KNLTTEKKVA
NLAPAVSDYT AYHHGEQALV QTIIGMAQNF VGTNNIYFLK PNGAFGTRAT GGKDAAAARY
IYTELNKIAR KVFHPADDPL FRYVQEDEKT VEPEWYLPVV PMVLINGAEG IGTGWSTSIP
PFNPLDVVNN IRHLLNDEEM DDMHPWFRGW TGTMEKIESQ RYRMYGRIEQ VGPNTLEITE
LPARTWTSTI KEHLLLGLGG SEKVKPWIKD MEEQHAETIK FIIKLTDEEM TKTRKLGFYE
RFKLISPISL QNMVAFDYRG KIKKYDHVHE ILKDFYEVRL EYYQKRKDYM TGRLQWEAEK
LSFQVKFIKM IIDKSLIVTN KPKKQLISEL EELGFPRINK EGKPHFGKID EEVEAIISED
EDEDLEESEE ATRKKDKDDE STVNGPEELF GTYEYLLGLK IWSLTKERYE KLLKQKQEKE
TELENLLKLS AKDLWNNDLD DFLTAYEDFQ KMDLFLRNSA VPKTKGGKRK RKGGDDDDYD
PSGKKKPARR IKKIKKEDDF DRILIKPQAK IKAKRPVKVK VEPPSSAAST PSVKEELGVS
DVTSNASTPS TTIFDQKVKQ ENSDESGISA FSSKFNKIAS AFDEDAPLDQ ITSEDTSVKE
SSAPAAKKKA PPKRKAKVVE SSEDELSDAN LSEQDDEEVV PVRRQRSSRQ TAKKSYAEPI
EISDEEDFID DDEDEEVDSD ESFNDE
