ID   TOP3B_DROME             Reviewed;         875 AA.
AC   O96651; Q5U0X6; Q9W416;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=DNA topoisomerase 3-beta;
DE            EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10131};
DE   AltName: Full=DNA topoisomerase III beta;
GN   Name=Top3beta; Synonyms=TOP3; ORFNames=CG3458;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=10636841; DOI=10.1074/jbc.275.3.1533;
RA   Wilson T.M., Chen A.D., Hsieh T.-S.;
RT   "Cloning and characterization of Drosophila topoisomerase IIIbeta.
RT   Relaxation of hypernegatively supercoiled DNA.";
RL   J. Biol. Chem. 275:1533-1540(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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). Weakly relaxes
CC       negative supercoils and displays a distinct preference for binding
CC       single-stranded DNA. {ECO:0000250, ECO:0000269|PubMed:10636841}.
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   -!- DEVELOPMENTAL STAGE: Expressed during the first 6 hours of embryonic
CC       development, levels decline during larval and pupal stages to increase
CC       again during adulthood. {ECO:0000269|PubMed:10636841}.
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01383, ECO:0000305}.
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DR   EMBL; AF099909; AAD13219.1; -; mRNA.
DR   EMBL; AE014298; AAF46144.1; -; Genomic_DNA.
DR   EMBL; BT016116; AAV37001.1; -; mRNA.
DR   RefSeq; NP_001284938.1; NM_001298009.1.
DR   RefSeq; NP_511059.2; NM_078504.4.
DR   AlphaFoldDB; O96651; -.
DR   SMR; O96651; -.
DR   BioGRID; 58054; 4.
DR   DIP; DIP-22155N; -.
DR   IntAct; O96651; 1.
DR   MINT; O96651; -.
DR   STRING; 7227.FBpp0309042; -.
DR   PaxDb; 7227-FBpp0070891; -.
DR   EnsemblMetazoa; FBtr0070930; FBpp0070891; FBgn0026015.
DR   EnsemblMetazoa; FBtr0340028; FBpp0309042; FBgn0026015.
DR   GeneID; 31565; -.
DR   KEGG; dme:Dmel_CG3458; -.
DR   AGR; FB:FBgn0026015; -.
DR   CTD; 31565; -.
DR   FlyBase; FBgn0026015; Top3beta.
DR   VEuPathDB; VectorBase:FBgn0026015; -.
DR   eggNOG; KOG1957; Eukaryota.
DR   HOGENOM; CLU_002929_1_0_1; -.
DR   InParanoid; O96651; -.
DR   OMA; KGKTAYG; -.
DR   OrthoDB; 166270at2759; -.
DR   PhylomeDB; O96651; -.
DR   BioGRID-ORCS; 31565; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 31565; -.
DR   PRO; PR:O96651; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0026015; Expressed in adult Malpighian tubule (Drosophila) and 25 other cell types or tissues.
DR   ExpressionAtlas; O96651; baseline and differential.
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; IDA:FlyBase.
DR   GO; GO:0006265; P:DNA topological change; IDA:FlyBase.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IMP:FlyBase.
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:SF20; DNA TOPOISOMERASE 3-BETA-1; 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.
DR   Genevisible; O96651; DM.
PE   2: Evidence at transcript level;
KW   DNA-binding; Isomerase; Reference proteome; Topoisomerase.
FT   CHAIN           1..875
FT                   /note="DNA topoisomerase 3-beta"
FT                   /id="PRO_0000145196"
FT   DOMAIN          3..153
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   DOMAIN          170..589
FT                   /note="Topo IA-type catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
FT   REGION          371..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        332
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
FT   CONFLICT        747
FT                   /note="V -> M (in Ref. 1; AAD13219)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   875 AA;  96973 MW;  3A26520C10AB6057 CRC64;
     MKSVLMVAEK PSLAASLAGI LSNGRCTAKR GTGNGCSTHE WTGNFRNEGS VHFRMTSVCG
     HVMSLDFNKK YNCWDKVDPI QLFGCATEKK ETNPKQNMRK FLAHEARGCD YLVLWLDCDK
     EGENICFEVM DAVKHVINNV YSDQVTYRAH FSAITEKDIK KAMETLGHPN ENEAKSVDAR
     QELDLRIGCA FTRFQTKFFQ DRYGDLDSSL ISYGPCQTPT LGFCVKRHDD IQTFKPESFW
     HLQLLAGQPE VTLEWARGRV FKKDIAIMLL NRVKEHKKAT VESVASKEAY KSKPQALNTV
     ELMRICSSGL GIGPFQAMQI AERLYTQGYI SYPRTETNQY PTNFDLPAVL HVLKPSADFG
     EEARSILGDI QTPRKGKDAG DHPPITPMKL GNRSDFDRDT WRVYEFICRH FMGTVSRDLK
     YRVTTAKLSV GMETFSCTAS VLIDAGFTKV MTWSAFGKDE PQPPFVQGTQ VAINDVRLIE
     SQTGPPDYLT ESELITLMEE HGIGTDASIP VHINNICQRN YVHIENGRKL MPTTLGIVLV
     HGYQKIDPEL VLPTMRTEVE RMLTLIAQGS ANFQDVLRHA IKIFKLKFMY FVKNIDSMDA
     LFEVSFSPLA ESGKAHSRCG KCRRYMKYIQ TKPARLHCSH CDETYALPIG NVKVYREFKC
     PLDDFDLLAF STGVKGRSYP FCPYCYNHPP FSDMPHLGGC NTCTNANCPH SLNTLGISSC
     VECPTGVLVL DCTLAPTWKL GCNRCDVIIN CFKGATKITV EEAKCQECGA QQVNVVYKSD
     KSKFKDGSEE KSGCIFCSAD FSHLVEKHRA VASRPVRSGG GFRGGKAGRG GGGMGGAAFG
     SGGAVTAGGG PNAGGGVRGS RVAKDKMGQL ASYFV
//