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O60126 (TOP3_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA topoisomerase 3

EC=5.99.1.2
Alternative name(s):
DNA topoisomerase III
Gene names
Name:top3
ORF Names:SPBC16G5.12c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length622 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone By similarity.

Catalytic activity

ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.

Subunit structure

Interacts with hus2. Ref.3

Sequence similarities

Belongs to the type IA topoisomerase family.

Contains 1 Toprim domain.

Ontologies

Keywords
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionIsomerase
Topoisomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA metabolic process

Inferred from genetic interaction PubMed 12409469. Source: PomBase

DNA topological change

Inferred from electronic annotation. Source: InterPro

maintenance of rDNA

Inferred from mutant phenotype PubMed 15340008. Source: PomBase

mitotic sister chromatid segregation

Inferred from mutant phenotype PubMed 10497270. Source: PomBase

nuclear cell cycle DNA replication

Inferred from mutant phenotype PubMed 12235386. Source: PomBase

nucleolus organization

Inferred from mutant phenotype PubMed 15340008. Source: PomBase

postreplication repair

Inferred from genetic interaction Ref.3. Source: PomBase

resolution of meiotic recombination intermediates

Traceable author statement PubMed 15340008. Source: PomBase

   Cellular_componentRecQ helicase-Topo III complex

Inferred from direct assay Ref.3. Source: PomBase

mitochondrion

Inferred from direct assay PubMed 16823372. Source: PomBase

nucleus

Inferred from direct assay Ref.3. Source: PomBase

site of double-strand break

Inferred from direct assay PubMed 23628481. Source: PomBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA topoisomerase type I activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 622622DNA topoisomerase 3
PRO_0000145197

Regions

Domain2 – 148147Toprim

Sites

Active site3301O-(5'-phospho-DNA)-tyrosine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
O60126 [UniParc].

Last modified May 1, 1999. Version 2.
Checksum: EF291B1717EB58C0

FASTA62271,169
        10         20         30         40         50         60 
MRVLCVAEKN SIAKSVASIL GGGHVRRRDT RSKYVKNYDF SFNFGGNVGS SDVTMTSVSG 

        70         80         90        100        110        120 
HLTEASFPSE YSSWSSVPQD VLFDAQIITS VSKNAEVLAD NIKKEARNAQ YLYIWTDCDR 

       130        140        150        160        170        180 
EGEHIGVEIS NVARASNPSI QVIRADFNNL ERSHIISAAK RPRDVSKNAA DAVDARIELD 

       190        200        210        220        230        240 
FRLGAIFTRL QTIQLQKSFD ILQNKIISYG PCQFPTLGFV VDRWQRVEDF VPETYWHLRF 

       250        260        270        280        290        300 
VDKRQGKTIQ FNWERAKVFD RLTTMIILEN CLECKTAKVV NITQKPKTKY KPLPLSTVEL 

       310        320        330        340        350        360 
TKLGPKHLRI SAKKTLELAE NLYTNGFVSY PRTETDQFDS SMNLHAIIQK LTGAQEWDSY 

       370        380        390        400        410        420 
AEGLLAGDYR PPRKGKHNDR AHPPIHPVQM VHRSALPSQD HWKVYELITR RFLACCSDNA 

       430        440        450        460        470        480 
KGAETLVQVK MEEELFSKKG LLVTEKNYLE VYPYEKWESS DQLPEYRLHE EFQPHILDMM 

       490        500        510        520        530        540 
DSSTSSPSYI TEPELIALMD ANGIGTDATM AEHIEKVQER EYVIKRKKRG QGVTEFVPSS 

       550        560        570        580        590        600 
LGVALAKGYD EIGLEWSLTK PFLRKEMEVQ LKNIENGQLN RNVLVHMILT QFRDVFHLTK 

       610        620 
QRFDCLKNSC RVYLMSHNEP QT 

« Hide

References

« Hide 'large scale' references
[1]"The top3+ gene is essential in Schizosaccharomyces pombe and the lethality associated with its loss is caused by Rad12 helicase activity."
Maftahi M., Han C.S., Langston L.D., Hope J.C., Zigouras N., Freyer G.A.
Nucleic Acids Res. 27:4715-4724(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 972 / ATCC 24843.
[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. expand/collapse author list , 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]"Role for the fission yeast RecQ helicase in DNA repair in G2."
Laursen L.V., Ampatzidou E., Andersen A.H., Murray J.M.
Mol. Cell. Biol. 23:3692-3705(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUS2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF126287 mRNA. Translation: AAD22485.2.
CU329671 Genomic DNA. Translation: CAA19038.1.
PIRT39604.
RefSeqNP_596761.1. NM_001023781.2.

3D structure databases

ProteinModelPortalO60126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276427. 12 interactions.
MINTMINT-4677412.
STRING4896.SPBC16G5.12c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC16G5.12c.1; SPBC16G5.12c.1:pep; SPBC16G5.12c.
GeneID2539881.
KEGGspo:SPBC16G5.12c.

Organism-specific databases

PomBaseSPBC16G5.12c.

Phylogenomic databases

eggNOGCOG0550.
HOGENOMHOG000184377.
KOK03165.
OMARNYLDIY.
OrthoDBEOG7Q8CWW.
PhylomeDBO60126.

Family and domain databases

Gene3D1.10.290.10. 1 hit.
1.10.460.10. 2 hits.
3.40.50.140. 1 hit.
InterProIPR000380. Topo_IA.
IPR003601. Topo_IA_2.
IPR023406. Topo_IA_AS.
IPR013497. Topo_IA_cen.
IPR013824. Topo_IA_cen_sub1.
IPR013826. Topo_IA_cen_sub3.
IPR023405. Topo_IA_core_domain.
IPR003602. Topo_IA_DNA-bd.
IPR006171. Toprim_domain.
[Graphical view]
PANTHERPTHR11390. PTHR11390. 1 hit.
PfamPF01131. Topoisom_bac. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]
PRINTSPR00417. PRTPISMRASEI.
SMARTSM00437. TOP1Ac. 1 hit.
SM00436. TOP1Bc. 1 hit.
SM00493. TOPRIM. 1 hit.
[Graphical view]
SUPFAMSSF56712. SSF56712. 1 hit.
PROSITEPS00396. TOPOISOMERASE_I_PROK. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20801026.
PROO60126.

Entry information

Entry nameTOP3_SCHPO
AccessionPrimary (citable) accession number: O60126
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names