ID   TOP3_SCHPO              Reviewed;         622 AA.
AC   O60126;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=DNA topoisomerase 3;
DE            EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10131};
DE   AltName: Full=DNA topoisomerase III;
GN   Name=top3; ORFNames=SPBC16G5.12c;
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 [MRNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10572171; DOI=10.1093/nar/27.24.4715;
RA   Maftahi M., Han C.S., Langston L.D., Hope J.C., Zigouras N., Freyer G.A.;
RT   "The top3+ gene is essential in Schizosaccharomyces pombe and the lethality
RT   associated with its loss is caused by Rad12 helicase activity.";
RL   Nucleic Acids Res. 27:4715-4724(1999).
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   INTERACTION WITH HUS2.
RX   PubMed=12724426; DOI=10.1128/mcb.23.10.3692-3705.2003;
RA   Laursen L.V., Ampatzidou E., Andersen A.H., Murray J.M.;
RT   "Role for the fission yeast RecQ helicase in DNA repair in G2.";
RL   Mol. Cell. Biol. 23:3692-3705(2003).
CC   -!- FUNCTION: Releases the supercoiling and torsional tension of DNA
CC       introduced during the DNA replication and transcription by transiently
CC       cleaving and rejoining one strand of the DNA duplex. Introduces a
CC       single-strand break via transesterification at a target site in duplex
CC       DNA. The scissile phosphodiester is attacked by the catalytic tyrosine
CC       of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-
CC       enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free
CC       DNA strand than undergoes passage around the unbroken strand thus
CC       removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH
CC       attacks the covalent intermediate to expel the active-site tyrosine and
CC       restore the DNA phosphodiester backbone (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC         passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10131};
CC   -!- SUBUNIT: Interacts with hus2. {ECO:0000269|PubMed:12724426}.
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01383, ECO:0000305}.
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DR   EMBL; AF126287; AAD22485.2; -; mRNA.
DR   EMBL; CU329671; CAA19038.1; -; Genomic_DNA.
DR   PIR; T39604; T39604.
DR   RefSeq; NP_596761.1; NM_001023781.2.
DR   AlphaFoldDB; O60126; -.
DR   SMR; O60126; -.
DR   BioGRID; 276427; 13.
DR   STRING; 284812.O60126; -.
DR   MaxQB; O60126; -.
DR   PaxDb; 4896-SPBC16G5-12c-1; -.
DR   EnsemblFungi; SPBC16G5.12c.1; SPBC16G5.12c.1:pep; SPBC16G5.12c.
DR   GeneID; 2539881; -.
DR   KEGG; spo:SPBC16G5.12c; -.
DR   PomBase; SPBC16G5.12c; top3.
DR   VEuPathDB; FungiDB:SPBC16G5.12c; -.
DR   eggNOG; KOG1956; Eukaryota.
DR   HOGENOM; CLU_002929_1_1_1; -.
DR   InParanoid; O60126; -.
DR   OMA; KGKTAYG; -.
DR   PhylomeDB; O60126; -.
DR   PRO; PR:O60126; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0031422; C:RecQ family helicase-topoisomerase III complex; IDA:PomBase.
DR   GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR   GO; GO:0003677; F:DNA binding; ISM:PomBase.
DR   GO; GO:0003916; F:DNA topoisomerase activity; IBA:GO_Central.
DR   GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; TAS:PomBase.
DR   GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR   GO; GO:0043007; P:maintenance of rDNA; IMP:PomBase.
DR   GO; GO:1902969; P:mitotic DNA replication; IMP:PomBase.
DR   GO; GO:0006301; P:postreplication repair; IGI:PomBase.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; TAS:PomBase.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR   Gene3D; 3.40.50.140; -; 1.
DR   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR   Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR   Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR   InterPro; IPR000380; Topo_IA.
DR   InterPro; IPR003601; Topo_IA_2.
DR   InterPro; IPR023406; Topo_IA_AS.
DR   InterPro; IPR013497; Topo_IA_cen.
DR   InterPro; IPR013824; Topo_IA_cen_sub1.
DR   InterPro; IPR013825; Topo_IA_cen_sub2.
DR   InterPro; IPR013826; Topo_IA_cen_sub3.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034144; TOPRIM_TopoIII.
DR   PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   PROSITE; PS00396; TOPO_IA_1; 1.
DR   PROSITE; PS52039; TOPO_IA_2; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Isomerase; Reference proteome; Topoisomerase.
FT   CHAIN           1..622
FT                   /note="DNA topoisomerase 3"
FT                   /id="PRO_0000145197"
FT   DOMAIN          2..148
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   DOMAIN          166..596
FT                   /note="Topo IA-type catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
FT   ACT_SITE        330
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
SQ   SEQUENCE   622 AA;  71169 MW;  EF291B1717EB58C0 CRC64;
     MRVLCVAEKN SIAKSVASIL GGGHVRRRDT RSKYVKNYDF SFNFGGNVGS SDVTMTSVSG
     HLTEASFPSE YSSWSSVPQD VLFDAQIITS VSKNAEVLAD NIKKEARNAQ YLYIWTDCDR
     EGEHIGVEIS NVARASNPSI QVIRADFNNL ERSHIISAAK RPRDVSKNAA DAVDARIELD
     FRLGAIFTRL QTIQLQKSFD ILQNKIISYG PCQFPTLGFV VDRWQRVEDF VPETYWHLRF
     VDKRQGKTIQ FNWERAKVFD RLTTMIILEN CLECKTAKVV NITQKPKTKY KPLPLSTVEL
     TKLGPKHLRI SAKKTLELAE NLYTNGFVSY PRTETDQFDS SMNLHAIIQK LTGAQEWDSY
     AEGLLAGDYR PPRKGKHNDR AHPPIHPVQM VHRSALPSQD HWKVYELITR RFLACCSDNA
     KGAETLVQVK MEEELFSKKG LLVTEKNYLE VYPYEKWESS DQLPEYRLHE EFQPHILDMM
     DSSTSSPSYI TEPELIALMD ANGIGTDATM AEHIEKVQER EYVIKRKKRG QGVTEFVPSS
     LGVALAKGYD EIGLEWSLTK PFLRKEMEVQ LKNIENGQLN RNVLVHMILT QFRDVFHLTK
     QRFDCLKNSC RVYLMSHNEP QT
//