TOP3B_DROME
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 03-AUG-2022, entry version 162.
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. {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.FBpp0070891; -.
DR PaxDb; O96651; -.
DR PRIDE; O96651; -.
DR EnsemblMetazoa; FBtr0070930; FBpp0070891; FBgn0026015.
DR EnsemblMetazoa; FBtr0340028; FBpp0309042; FBgn0026015.
DR GeneID; 31565; -.
DR KEGG; dme:Dmel_CG3458; -.
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; TYPRVDT; -.
DR OrthoDB; 373433at2759; -.
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 tissues.
DR ExpressionAtlas; O96651; baseline and differential.
DR Genevisible; O96651; DM.
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; 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 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 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:0000250"
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
