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Protein

DNA topoisomerase 2

Gene

top2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.

Catalytic activityi

ATP-dependent breakage, passage and rejoining of double-stranded DNA.PROSITE-ProRule annotation

Cofactori

Mg2+PROSITE-ProRule annotation, Mn2+PROSITE-ProRule annotation, Ca2+PROSITE-ProRule annotationNote: Binds two Mg2+ per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn2+ or Ca2+.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei136 – 1361ATPBy similarity
Binding sitei165 – 1651ATPBy similarity
Metal bindingi505 – 5051Magnesium 1; catalyticPROSITE-ProRule annotation
Metal bindingi582 – 5821Magnesium 1; catalyticPROSITE-ProRule annotation
Metal bindingi582 – 5821Magnesium 2PROSITE-ProRule annotation
Metal bindingi584 – 5841Magnesium 2PROSITE-ProRule annotation
Sitei834 – 8341Transition state stabilizerBy similarity
Active sitei835 – 8351O-(5'-phospho-DNA)-tyrosine intermediateBy similarity
Sitei886 – 8861Important for DNA bending; intercalates between base pairs of target DNABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi193 – 1953ATPBy similarity
Nucleotide bindingi206 – 2138ATPBy similarity
Nucleotide bindingi421 – 4233ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: PomBase
  • DNA binding Source: UniProtKB-KW
  • DNA topoisomerase type II (ATP-hydrolyzing) activity Source: PomBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • chromatin organization Source: PomBase
  • DNA strand elongation involved in mitotic DNA replication Source: PomBase
  • DNA topological change Source: PomBase
  • DNA unwinding involved in DNA replication Source: GO_Central
  • mitotic DNA integrity checkpoint Source: GO_Central
  • mitotic recombination Source: GO_Central
  • mitotic sister chromatid separation Source: PomBase
  • resolution of meiotic recombination intermediates Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Topoisomerase

Keywords - Ligandi

ATP-binding, DNA-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-4615885. SUMOylation of DNA replication proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA topoisomerase 2 (EC:5.99.1.3)
Alternative name(s):
DNA topoisomerase II
Gene namesi
Name:top2
ORF Names:SPBC1A4.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1A4.03c.
PomBaseiSPBC1A4.03c. top2.

Subcellular locationi

GO - Cellular componenti

  • chromosome, centromeric core domain Source: PomBase
  • DNA topoisomerase complex (ATP-hydrolyzing) Source: GO_Central
  • nuclear chromosome Source: PomBase
  • nucleus Source: PomBase
  • transcriptionally active chromatin Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14851485DNA topoisomerase 2PRO_0000145386Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1310 – 13101Phosphoserine1 Publication
Modified residuei1345 – 13451Phosphoserine1 Publication
Modified residuei1433 – 14331Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated at multiple sites at both extremities of the protein.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP08096.

PTM databases

iPTMnetiP08096.

Interactioni

Subunit structurei

Homodimer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei533 – 5331Interaction with DNAPROSITE-ProRule annotation
Sitei536 – 5361Interaction with DNAPROSITE-ProRule annotation
Sitei703 – 7031Interaction with DNAPROSITE-ProRule annotation
Sitei704 – 7041Interaction with DNAPROSITE-ProRule annotation
Sitei753 – 7531Interaction with DNAPROSITE-ProRule annotation
Sitei787 – 7871Interaction with DNAPROSITE-ProRule annotation
Sitei793 – 7931Interaction with DNAPROSITE-ProRule annotation
Sitei961 – 9611Interaction with DNAPROSITE-ProRule annotation

Protein-protein interaction databases

BioGridi277068. 20 interactions.
MINTiMINT-4687024.

Structurei

3D structure databases

ProteinModelPortaliP08096.
SMRiP08096. Positions 74-448, 476-1204.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini499 – 613115ToprimPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni388 – 3925Interaction with DNABy similarity
Regioni1019 – 102810Interaction with DNABy similarity

Sequence similaritiesi

Belongs to the type II topoisomerase family.Curated
Contains 1 Toprim domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000216693.
InParanoidiP08096.
KOiK03164.
OMAiKDCASAR.
OrthoDBiEOG7CCC0D.
PhylomeDBiP08096.

Family and domain databases

Gene3Di1.10.268.10. 1 hit.
3.30.1360.40. 1 hit.
3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
3.40.50.670. 1 hit.
3.90.199.10. 1 hit.
InterProiIPR024946. Arg_repress_C-like.
IPR003594. HATPase_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR001241. Topo_IIA.
IPR013760. Topo_IIA-like_dom.
IPR002205. Topo_IIA_A/C.
IPR013758. Topo_IIA_A/C_ab.
IPR013757. Topo_IIA_A_a.
IPR013506. Topo_IIA_bsu_dom2.
IPR013759. Topo_IIA_cen_dom.
IPR018522. TopoIIA_CS.
IPR031660. TOPRIM_C.
IPR006171. Toprim_domain.
[Graphical view]
PfamiPF00204. DNA_gyraseB. 1 hit.
PF00521. DNA_topoisoIV. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
PF16898. TOPRIM_C. 1 hit.
[Graphical view]
PRINTSiPR00418. TPI2FAMILY.
SMARTiSM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
SM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
PROSITEiPS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08096-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIDADFSDY EDEASGDENV LPNTTTKRKA STTSSKSRAK KASTPDLRQT
60 70 80 90 100
SLTSMTASEQ IPLVTNNGNG NSNVSTQYQR LTPREHVLRR PDTYIGSIEP
110 120 130 140 150
TTSEMWVFDS EKNKLDYKAV TYVPGLYKIF DEIIVNAADN KVRDPNMNTL
160 170 180 190 200
KVTLDPEANV ISIYNNGKGI PIEIHDKEKI YIPELIFGNL LTSSNYDDNQ
210 220 230 240 250
KKVTGGRNGY GAKLCNIFST EFVVETADKE RMKKYKQTWY DNMSRKSEPV
260 270 280 290 300
ITSLKKPDEY TKITFKPDLA KFGMDKIDDD MVSIIKRRIY DMAGTVRETK
310 320 330 340 350
VYLNNERISI SGFKKYVEMY LASDTKPDEE PPRVIYEHVN DRWDVAFAVS
360 370 380 390 400
DGQFKQVSFV NNISTIRGGT HVNYVANKIV DAIDEVVKKE NKKAPVKAFQ
410 420 430 440 450
IKNYVQVFVN CQIENPSFDS QTKETLTTKV SAFGSQCTLS DKFLKAIKKS
460 470 480 490 500
SVVEEVLKFA TAKADQQLSK GDGGLRSRIT GLTKLEDANK AGTKESHKCV
510 520 530 540 550
LILTEGDSAK SLAVSGLSVV GRDYYGVFPL RGKLLNVREA SHSQILNNKE
560 570 580 590 600
IQAIKKIMGF THKKTYTDVK GLRYGHLMIM TDQDHDGSHI KGLIINYLES
610 620 630 640 650
SYPSLLQIPG FLIQFITPII KCTRGNQVQA FYTLPEYEYW KEANNNGRGW
660 670 680 690 700
KIKYYKGLGT SDHDDMKSYF SDLDRHMKYF HAMQEKDAEL IEMAFAKKKA
710 720 730 740 750
DVRKEWLRTY RPGIYMDYTQ PQIPIDDFIN RELIQFSMAD NIRSIPSVVD
760 770 780 790 800
GLKPGQRKVV YYCFKRNLVH ETKVSRLAGY VASETAYHHG EVSMEQTIVN
810 820 830 840 850
LAQNFVGSNN INLLMPNGQF GTRSEGGKNA SASRYLNTAL SPLARVLFNS
860 870 880 890 900
NDDQLLNYQN DEGQWIEPEY YVPILPMVLV NGAEGIGTGW STFIPNYNPK
910 920 930 940 950
DITANLRHML NGEPLEIMTP WYRGFRGSIT KVAPDRYKIS GIINQIGENK
960 970 980 990 1000
VEITELPIRF WTQDMKEYLE AGLVGTEKIR KFIVDYESHH GEGNVHFNVT
1010 1020 1030 1040 1050
LTEAGMKEAL NESLEVKFKL SRTQATSNMI AFDASGRIKK YDSVEDILTE
1060 1070 1080 1090 1100
FYEVRLRTYQ RRKEHMVNEL EKRFDRFSNQ ARFIHMIIEG ELVVSKKKKK
1110 1120 1130 1140 1150
DLIVELKEKK FQPISKPKKG HLVDLEVENA LAEEEQSGDV SQDEDSDAYN
1160 1170 1180 1190 1200
YLLSMPLWSL TYERYVELLK KKDEVMAELD ALIKKTPKEL WLHDLDAFEH
1210 1220 1230 1240 1250
AWNKVMDDIQ REMLEEEQSS RDFVNRTKKK PRGKSTGTRK PRAIAGSSSS
1260 1270 1280 1290 1300
TAVKKEASSE SKPSTTNRKQ QTLLEFAASK EPEKSSDINI VKTEDNSHGL
1310 1320 1330 1340 1350
SVEENRISKS PGLDSSDSGK SRKRSQSVDS EDAGSKKPVK KIAASASGRG
1360 1370 1380 1390 1400
RKTNKPVATT IFSSDDEDDL LPSSLKPSTI TSTKASAKNK GKKASSVKKQ
1410 1420 1430 1440 1450
SPEDDDDDFI IPGSSSTPKA SSTNAEPPED SDSPIRKRPT RRAAATVKTP
1460 1470 1480
IYVDPSFDSM DEPSMQDDSF IVDNDEDVDD YDESD
Length:1,485
Mass (Da):167,892
Last modified:January 11, 2001 - v2
Checksum:i6D88F76243361B2F
GO

Sequence cautioni

The sequence CAA27857.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti994 – 9941N → I in CAA27857 (PubMed:3023070).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04326 Genomic DNA. Translation: CAA27857.1. Different initiation.
CU329671 Genomic DNA. Translation: CAA20107.1.
PIRiT39851. ISZPT2.
RefSeqiNP_595805.1. NM_001021708.2.

Genome annotation databases

EnsemblFungiiSPBC1A4.03c.1; SPBC1A4.03c.1:pep; SPBC1A4.03c.
GeneIDi2540541.
KEGGispo:SPBC1A4.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04326 Genomic DNA. Translation: CAA27857.1. Different initiation.
CU329671 Genomic DNA. Translation: CAA20107.1.
PIRiT39851. ISZPT2.
RefSeqiNP_595805.1. NM_001021708.2.

3D structure databases

ProteinModelPortaliP08096.
SMRiP08096. Positions 74-448, 476-1204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277068. 20 interactions.
MINTiMINT-4687024.

PTM databases

iPTMnetiP08096.

Proteomic databases

MaxQBiP08096.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1A4.03c.1; SPBC1A4.03c.1:pep; SPBC1A4.03c.
GeneIDi2540541.
KEGGispo:SPBC1A4.03c.

Organism-specific databases

EuPathDBiFungiDB:SPBC1A4.03c.
PomBaseiSPBC1A4.03c. top2.

Phylogenomic databases

HOGENOMiHOG000216693.
InParanoidiP08096.
KOiK03164.
OMAiKDCASAR.
OrthoDBiEOG7CCC0D.
PhylomeDBiP08096.

Enzyme and pathway databases

ReactomeiR-SPO-4615885. SUMOylation of DNA replication proteins.

Miscellaneous databases

PROiP08096.

Family and domain databases

Gene3Di1.10.268.10. 1 hit.
3.30.1360.40. 1 hit.
3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
3.40.50.670. 1 hit.
3.90.199.10. 1 hit.
InterProiIPR024946. Arg_repress_C-like.
IPR003594. HATPase_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR001241. Topo_IIA.
IPR013760. Topo_IIA-like_dom.
IPR002205. Topo_IIA_A/C.
IPR013758. Topo_IIA_A/C_ab.
IPR013757. Topo_IIA_A_a.
IPR013506. Topo_IIA_bsu_dom2.
IPR013759. Topo_IIA_cen_dom.
IPR018522. TopoIIA_CS.
IPR031660. TOPRIM_C.
IPR006171. Toprim_domain.
[Graphical view]
PfamiPF00204. DNA_gyraseB. 1 hit.
PF00521. DNA_topoisoIV. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
PF16898. TOPRIM_C. 1 hit.
[Graphical view]
PRINTSiPR00418. TPI2FAMILY.
SMARTiSM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
SM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
PROSITEiPS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of the fission yeast DNA topoisomerase II gene: structural and functional relationships to other DNA topoisomerases."
    Uemura T., Morikawa K., Yanagida M.
    EMBO J. 5:2355-2361(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "A functional 125-kDa core polypeptide of fission yeast DNA topoisomerase II."
    Shiozaki K., Yanagida M.
    Mol. Cell. Biol. 11:6093-6102(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS.
  4. "Functional dissection of the phosphorylated termini of fission yeast DNA topoisomerase II."
    Shiozaki K., Yanagida M.
    J. Cell Biol. 119:1023-1036(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS, PHOSPHORYLATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1310; SER-1345 AND SER-1433, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiTOP2_SCHPO
AccessioniPrimary (citable) accession number: P08096
Secondary accession number(s): O74336
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 11, 2001
Last modified: July 6, 2016
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.