ID TOP2_PICGU Reviewed; 1400 AA.
AC Q01879; A5DL75; Q9HGH1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 24-JAN-2024, entry version 131.
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; ORFNames=PGUG_04026;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 93-874.
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324,
RC NUM249, NUM4, and NUM43;
RX PubMed=11470534; DOI=10.1016/s0378-1119(01)00526-1;
RA Kato M., Ozeki M., Kikuchi A., Kanbe T.;
RT "Phylogenetic relationship and mode of evolution of yeast DNA topoisomerase
RT II gene in the pathogenic Candida species.";
RL Gene 272:275-281(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1042-1400.
RC STRAIN=L2;
RA Boretsky Y.R., Liauta-Teglivets O.Y., Hasslacher M., Voronovsky A.,
RA Kohlwein S.D., Shavlovsky G.M.;
RL Submitted (JUL-1996) 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.
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA99278.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA99278.1; Type=Erroneous translation; Note=Wrong genetic code used for translating the sequence.; Evidence={ECO:0000305};
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DR EMBL; CH408159; EDK39928.2; -; Genomic_DNA.
DR EMBL; AB049145; BAB13754.2; -; Genomic_DNA.
DR EMBL; Z74991; CAA99278.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001483297.1; XM_001483247.1.
DR AlphaFoldDB; Q01879; -.
DR SMR; Q01879; -.
DR STRING; 294746.Q01879; -.
DR GeneID; 5125173; -.
DR KEGG; pgu:PGUG_04026; -.
DR VEuPathDB; FungiDB:PGUG_04026; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_1_0_1; -.
DR InParanoid; Q01879; -.
DR OMA; NESMDYN; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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; cd16930; HATPase_TopII-like; 1.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.1490.30; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_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; IPR001154; TopoII_euk.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034157; TOPRIM_TopoII.
DR PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
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 PRINTS; PR01158; TOPISMRASEII.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS52040; TOPO_IIA; 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..1400
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145385"
FT DOMAIN 497..613
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT DOMAIN 749..1214
FT /note="Topo IIA-type catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01384"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..386
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT REGION 1019..1028
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT REGION 1235..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 839
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01384"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 174..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 187..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 415..417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 503
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 582
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 582
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 584
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 531
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 534
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 707
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 708
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 757
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 791
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 797
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 838
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 890
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
FT SITE 965
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT CONFLICT 1293
FT /note="L -> F (in Ref. 3; CAA99278)"
FT /evidence="ECO:0000305"
FT CONFLICT 1325
FT /note="I -> V (in Ref. 3; CAA99278)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1400 AA; 158157 MW; A032D0BB831775BB CRC64;
MSSFESDSAS DAESAFSDAS SDFTPSSSVK SKGKVPLRDS TNTTAQPSAP ATGDASDQYQ
KLSQLEHILK RPDTYIGSVE KTGVEMWSFD AATESMIYKE VHIVPGLYKI FDEILVNAAD
NKIRDPSMRN IKVNIDAENN TISVMNDGKG IPIEIHKKEK IYIPELIFGN LLTSSNYDDD
EKKVTGGRNG YGAKLCNIFS TEFVLETADL NTSQVYKQTW TNNMANLTKP KITKLKSKKE
YTKVTFKPDL SKFHMEMLDD DILSVLRRRV YDLCGTVKDC NIYLNDKKLS IRNFKSYVEM
YVNAIRERSP DPVAPEGETR NYSTIVHEVF NDRWEVAFAV SDGSFNQVSF VNSIATTSGG
THVKYVSDQI ITKLIDALTK KEKGKKKLNI KPQEVRNNMF VFINCLIENP AFTSQTKEQL
TTRVAQFGGK PSEKIVISDQ FIAKILKTSI ADKIRTIVNA NEDKEMSKAD GSRKSRIKNQ
VKLVDANKAG TKEGYKCTLI LTEGDSAMPL AVAGLTVVGR DYYGCFPLRG KLLNVREASI
EQVSKNAEIN SIKQIMGLQH KKRYTPENIK SLRYGHIMIM TDQDQDGSHI KGLIINFLET
SFPGLLEIPG FLLEFITPIV KVTITGRGNH RVIPFYNMPE FEKWRETEGT TCKWKHKYFK
GLGTSLESEG REYFAALDRH MKSFHALQDG DSQYIDMAFS KKKADERKDW LQAFRPGTHL
DPQIREIPIS EFINKELILF SMADNVRSIP SILDGFKPGQ RKVLYGCFKR NLRSEIKVAQ
LVGYISEHTG YHHGEGSLAQ TIVGLAQNFV GANNLNLLQP IGLFGSRAAG GKDFSAVRYI
HTNITDLTRV IFNPLDDDLY TYVQDDAQTV EPEAYLPIIP MLLVNGAEGI GTGWSTNIPS
FNPVDIVANI RRMMNGEEPV DMTPWFKGWE GDLERISPEK YKVSGKIEQV DDDTVEITEI
PIKTWTNSVK EFLLAGLGND KPWIKDMEEQ HGINIRFVVR LSKEEMDKSL RMGLLERFKL
ISSISLSNMV AFDPQGRIKK YSSANEILKD YYWARLELYQ RRKDMMAENF QNQLTRLSEQ
ARFIKLIIEK KLTIANKKRS EMVDDLKKLK FTRFNKNGKP VHDEPLVEAE ELAEEEEEAA
GDISQLNLGL VAPEDESQYK PETTYSQYDY LLGMAIWSLT RERYEKLLRQ RDEKQEELNE
LLKKSAKDLW NSDLDDFLVG WEEFLRADIE ARNSFGPTAK TSTRKRARKS TKSEPAQKKT
KSSTPKASTP TIKAEATPAQ PVVKEETNKQ PDLLSFFSKE PSVAKTVSAA PPKRKTPKSK
PKKEIVSLFS DSSDDDITSF SVGDAKPTPK PSTNNILDEL EDLKSSTFTP KVGAAGRRRP
KSYALAESDG NESDEDYMSE
//
