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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)DescriptionActionsGraphical viewLength
Binding sitei136ATPBy similarity1
Binding sitei165ATPBy similarity1
Metal bindingi505Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi582Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi582Magnesium 2PROSITE-ProRule annotation1
Metal bindingi584Magnesium 2PROSITE-ProRule annotation1
Sitei834Transition state stabilizerBy similarity1
Active sitei835O-(5'-phospho-DNA)-tyrosine intermediateBy similarity1
Sitei886Important for DNA bending; intercalates between base pairs of target DNABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi193 – 195ATPBy similarity3
Nucleotide bindingi206 – 213ATPBy similarity8
Nucleotide bindingi421 – 423ATPBy similarity3

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • 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
  • nucleus Source: PomBase
  • transcriptionally active chromatin Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001453861 – 1485DNA topoisomerase 2Add BLAST1485

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1310Phosphoserine1 Publication1
Modified residuei1345Phosphoserine1 Publication1
Modified residuei1433Phosphoserine1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP08096.
PRIDEiP08096.

PTM databases

iPTMnetiP08096.

Interactioni

Subunit structurei

Homodimer.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei533Interaction with DNAPROSITE-ProRule annotation1
Sitei536Interaction with DNAPROSITE-ProRule annotation1
Sitei703Interaction with DNAPROSITE-ProRule annotation1
Sitei704Interaction with DNAPROSITE-ProRule annotation1
Sitei753Interaction with DNAPROSITE-ProRule annotation1
Sitei787Interaction with DNAPROSITE-ProRule annotation1
Sitei793Interaction with DNAPROSITE-ProRule annotation1
Sitei961Interaction with DNAPROSITE-ProRule annotation1

Protein-protein interaction databases

BioGridi277068. 20 interactors.
MINTiMINT-4687024.

Structurei

3D structure databases

ProteinModelPortaliP08096.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini499 – 613ToprimPROSITE-ProRule annotationAdd BLAST115

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni388 – 392Interaction with DNABy similarity5
Regioni1019 – 1028Interaction with DNABy similarity10

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000216693.
InParanoidiP08096.
KOiK03164.
OMAiVCITELP.
OrthoDBiEOG092C08KH.
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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti994N → I in CAA27857 (PubMed:3023070).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277068. 20 interactors.
MINTiMINT-4687024.

PTM databases

iPTMnetiP08096.

Proteomic databases

MaxQBiP08096.
PRIDEiP08096.

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.
OMAiVCITELP.
OrthoDBiEOG092C08KH.
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...

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: November 30, 2016
This is version 160 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.