TOP2_SCHPO
ID TOP2_SCHPO Reviewed; 1485 AA.
AC P08096; O74336;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 197.
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=SPBC1A4.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3023070; DOI=10.1002/j.1460-2075.1986.tb04504.x;
RA Uemura T., Morikawa K., Yanagida M.;
RT "The nucleotide sequence of the fission yeast DNA topoisomerase II gene:
RT structural and functional relationships to other DNA topoisomerases.";
RL EMBO J. 5:2355-2361(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP DOMAINS.
RX PubMed=1658625; DOI=10.1128/mcb.11.12.6093-6102.1991;
RA Shiozaki K., Yanagida M.;
RT "A functional 125-kDa core polypeptide of fission yeast DNA topoisomerase
RT II.";
RL Mol. Cell. Biol. 11:6093-6102(1991).
RN [4]
RP DOMAINS, AND PHOSPHORYLATION.
RX PubMed=1332977; DOI=10.1083/jcb.119.5.1023;
RA Shiozaki K., Yanagida M.;
RT "Functional dissection of the phosphorylated termini of fission yeast DNA
RT topoisomerase II.";
RL J. Cell Biol. 119:1023-1036(1992).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1310; SER-1345 AND SER-1433,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 -!- PTM: Phosphorylated at multiple sites at both extremities of the
CC protein. {ECO:0000269|PubMed:1332977, ECO:0000269|PubMed:18257517}.
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=CAA27857.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X04326; CAA27857.1; ALT_INIT; Genomic_DNA.
DR EMBL; CU329671; CAA20107.1; -; Genomic_DNA.
DR PIR; T39851; ISZPT2.
DR RefSeq; NP_595805.1; NM_001021708.2.
DR AlphaFoldDB; P08096; -.
DR SMR; P08096; -.
DR BioGRID; 277068; 83.
DR STRING; 4896.SPBC1A4.03c.1; -.
DR iPTMnet; P08096; -.
DR MaxQB; P08096; -.
DR PaxDb; P08096; -.
DR PRIDE; P08096; -.
DR EnsemblFungi; SPBC1A4.03c.1; SPBC1A4.03c.1:pep; SPBC1A4.03c.
DR GeneID; 2540541; -.
DR KEGG; spo:SPBC1A4.03c; -.
DR PomBase; SPBC1A4.03c; top2.
DR VEuPathDB; FungiDB:SPBC1A4.03c; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_1_1_1; -.
DR InParanoid; P08096; -.
DR OMA; PMDDNIL; -.
DR PhylomeDB; P08096; -.
DR Reactome; R-SPO-4615885; SUMOylation of DNA replication proteins.
DR PRO; PR:P08096; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0034506; C:chromosome, centromeric core domain; IDA:PomBase.
DR GO; GO:0000791; C:euchromatin; IDA:PomBase.
DR GO; GO:0000228; C:nuclear chromosome; NAS:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IC:PomBase.
DR GO; GO:0003677; F:DNA binding; ISM:PomBase.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IGI:PomBase.
DR GO; GO:0006265; P:DNA topological change; IMP:PomBase.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:PomBase.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IGI:PomBase.
DR GO; GO:0000819; P:sister chromatid segregation; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Topoisomerase.
FT CHAIN 1..1485
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145386"
FT DOMAIN 499..613
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..392
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 1216..1485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1468..1485
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 835
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 193..195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 421..423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 505
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 533
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 536
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 703
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 704
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 753
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 787
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 793
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 834
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 886
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
FT SITE 961
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT MOD_RES 1310
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1345
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1433
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 994
FT /note="N -> I (in Ref. 1; CAA27857)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1485 AA; 167892 MW; 6D88F76243361B2F CRC64;
MSIDADFSDY EDEASGDENV LPNTTTKRKA STTSSKSRAK KASTPDLRQT SLTSMTASEQ
IPLVTNNGNG NSNVSTQYQR LTPREHVLRR PDTYIGSIEP TTSEMWVFDS EKNKLDYKAV
TYVPGLYKIF DEIIVNAADN KVRDPNMNTL KVTLDPEANV ISIYNNGKGI PIEIHDKEKI
YIPELIFGNL LTSSNYDDNQ KKVTGGRNGY GAKLCNIFST EFVVETADKE RMKKYKQTWY
DNMSRKSEPV ITSLKKPDEY TKITFKPDLA KFGMDKIDDD MVSIIKRRIY DMAGTVRETK
VYLNNERISI SGFKKYVEMY LASDTKPDEE PPRVIYEHVN DRWDVAFAVS DGQFKQVSFV
NNISTIRGGT HVNYVANKIV DAIDEVVKKE NKKAPVKAFQ IKNYVQVFVN CQIENPSFDS
QTKETLTTKV SAFGSQCTLS DKFLKAIKKS SVVEEVLKFA TAKADQQLSK GDGGLRSRIT
GLTKLEDANK AGTKESHKCV LILTEGDSAK SLAVSGLSVV GRDYYGVFPL RGKLLNVREA
SHSQILNNKE IQAIKKIMGF THKKTYTDVK GLRYGHLMIM TDQDHDGSHI KGLIINYLES
SYPSLLQIPG FLIQFITPII KCTRGNQVQA FYTLPEYEYW KEANNNGRGW KIKYYKGLGT
SDHDDMKSYF SDLDRHMKYF HAMQEKDAEL IEMAFAKKKA DVRKEWLRTY RPGIYMDYTQ
PQIPIDDFIN RELIQFSMAD NIRSIPSVVD GLKPGQRKVV YYCFKRNLVH ETKVSRLAGY
VASETAYHHG EVSMEQTIVN LAQNFVGSNN INLLMPNGQF GTRSEGGKNA SASRYLNTAL
SPLARVLFNS NDDQLLNYQN DEGQWIEPEY YVPILPMVLV NGAEGIGTGW STFIPNYNPK
DITANLRHML NGEPLEIMTP WYRGFRGSIT KVAPDRYKIS GIINQIGENK VEITELPIRF
WTQDMKEYLE AGLVGTEKIR KFIVDYESHH GEGNVHFNVT LTEAGMKEAL NESLEVKFKL
SRTQATSNMI AFDASGRIKK YDSVEDILTE FYEVRLRTYQ RRKEHMVNEL EKRFDRFSNQ
ARFIHMIIEG ELVVSKKKKK DLIVELKEKK FQPISKPKKG HLVDLEVENA LAEEEQSGDV
SQDEDSDAYN YLLSMPLWSL TYERYVELLK KKDEVMAELD ALIKKTPKEL WLHDLDAFEH
AWNKVMDDIQ REMLEEEQSS RDFVNRTKKK PRGKSTGTRK PRAIAGSSSS TAVKKEASSE
SKPSTTNRKQ QTLLEFAASK EPEKSSDINI VKTEDNSHGL SVEENRISKS PGLDSSDSGK
SRKRSQSVDS EDAGSKKPVK KIAASASGRG RKTNKPVATT IFSSDDEDDL LPSSLKPSTI
TSTKASAKNK GKKASSVKKQ SPEDDDDDFI IPGSSSTPKA SSTNAEPPED SDSPIRKRPT
RRAAATVKTP IYVDPSFDSM DEPSMQDDSF IVDNDEDVDD YDESD
