TOP3_SCHPO
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 25-MAY-2022, entry version 149.
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. {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; 4896.SPBC16G5.12c.1; -.
DR MaxQB; O60126; -.
DR PaxDb; O60126; -.
DR PRIDE; O60126; -.
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; TYPRVDT; -.
DR PhylomeDB; O60126; -.
DR PRO; PR:O60126; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
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; 1.10.290.10; -; 1.
DR Gene3D; 1.10.460.10; -; 1.
DR Gene3D; 2.70.20.10; -; 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; PTHR11390; 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; SSF56712; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 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 ACT_SITE 330
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
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
