ID   TOP3_DICDI              Reviewed;         828 AA.
AC   Q8T2T7; Q554F7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=DDB_G0275257;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- SIMILARITY: Belongs to the type IA topoisomerase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000013; EAL69909.2; -; Genomic_DNA.
DR   RefSeq; XP_643754.2; XM_638662.2.
DR   AlphaFoldDB; Q8T2T7; -.
DR   SMR; Q8T2T7; -.
DR   STRING; 44689.DDB0234226; -.
DR   PaxDb; Q8T2T7; -.
DR   EnsemblProtists; EAL69909; EAL69909; DDB_G0275257.
DR   GeneID; 8619798; -.
DR   KEGG; ddi:DDB_G0275257; -.
DR   dictyBase; DDB_G0275257; top3.
DR   eggNOG; KOG1956; Eukaryota.
DR   HOGENOM; CLU_002929_1_2_1; -.
DR   InParanoid; Q8T2T7; -.
DR   OMA; EHICFEV; -.
DR   PhylomeDB; Q8T2T7; -.
DR   Reactome; R-DDI-5693607; Processing of DNA double-strand break ends.
DR   PRO; PR:Q8T2T7; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
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   3: Inferred from homology;
KW   DNA-binding; Isomerase; Reference proteome; Topoisomerase.
FT   CHAIN           1..828
FT                   /note="DNA topoisomerase 3"
FT                   /id="PRO_0000330480"
FT   DOMAIN          4..149
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   REGION          763..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        361
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   828 AA;  94639 MW;  C0F25439F30D5618 CRC64;
     MTKRILNVAE KPSAAKEIAA ILSNKRATVR EGFSKYNKLW DFKYNILNFN DCEMTFTSVT
     GHLMEIDVVE QFKPWASCDP IQLFDAPIRK TVPSDKEPLK KTLEREIKKA DILILWLDCD
     REGENIAFEV LEVCKNAKKK FEFYRAHFSA IIPREIDRAC KNLAKPNEKD SIAVDTRMEI
     DLRIGAAFTR FQTLYLKKFK IISNSDNQPK TTTPANGNIL NNSNNNSSGK EIISYGPCQF
     PTLGFVVERY FRIVNFKPED FWHLSVVHEK MDTSSGKMIP VTFSWCRNRL FDYTAAFILY
     EKCLDNTEAT VVDVTSKESR YRPVPLTTIE LQKAASKKLR ISSVQTMQYA EELYTKGLIS
     YPRTETDSFQ AGTDLKGLIG NQASNPEWGA YASRLINNNQ FVYPKSGKNN DNSHPPIHPT
     SSATGLSGNL KKIYDFITRR FLACCSEESV FANTTVTIDI QGERFSETGT MVLKLGYLEV
     YPFDKRNDKL IPTYQKGERF TPKRIDLTKG TTVAPHYITE AELLTAMDNN KIGTDATMAT
     HIQTIQDRFY VKKNESNQFV PSNLGVSLVA SYELMGFEFS KPNLRAAIEA DVDKISRGQK
     TKQEVLLSTI EKYKQLYQLA NQNINCFDRS FREYYEPADP KGGEFRVLVS QFSRCGKCNG
     KMQYKSDQNP EAPKRILFCP QCIDTFDLPK NGDISQLVTS MGVPQNCPIC QYQVLSVRNP
     INDKSYTICP KCRNSPPDPI HKKPFHCFQC TFNCNLATGN KQQQQQQQQQ QQQTNYNRNN
     NNNNTNSARP ITTRTTRTTT QHRTFTASNN NFNNNNRNSD RNNNNFIF