TOP3A_DROME
ID TOP3A_DROME Reviewed; 1250 AA.
AC Q9NG98; Q6AWG6; Q9VIV1;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=DNA topoisomerase 3-alpha;
DE EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10131};
DE AltName: Full=DNA topoisomerase III alpha;
GN Name=Top3alpha; ORFNames=CG10123;
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].
RC TISSUE=Embryo;
RA Plank J.L., Reineke J.C., Wilson T.M., Hsieh T.-S.;
RT "Drosophila melanogaster topoisomerase III alpha.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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 (AUG-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}.
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}.
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DR EMBL; AF255733; AAF71288.1; -; mRNA.
DR EMBL; AE014134; AAF53813.2; -; Genomic_DNA.
DR EMBL; BT015282; AAT94511.1; -; mRNA.
DR RefSeq; NP_523602.2; NM_078878.3.
DR AlphaFoldDB; Q9NG98; -.
DR SMR; Q9NG98; -.
DR IntAct; Q9NG98; 4.
DR MINT; Q9NG98; -.
DR STRING; 7227.FBpp0080787; -.
DR PaxDb; Q9NG98; -.
DR PRIDE; Q9NG98; -.
DR DNASU; 35236; -.
DR EnsemblMetazoa; FBtr0081246; FBpp0080787; FBgn0040268.
DR GeneID; 35236; -.
DR KEGG; dme:Dmel_CG10123; -.
DR CTD; 35236; -.
DR FlyBase; FBgn0040268; Top3alpha.
DR VEuPathDB; VectorBase:FBgn0040268; -.
DR eggNOG; KOG1956; Eukaryota.
DR GeneTree; ENSGT00940000156701; -.
DR HOGENOM; CLU_002929_1_2_1; -.
DR InParanoid; Q9NG98; -.
DR OMA; WYKTCLP; -.
DR OrthoDB; 373433at2759; -.
DR PhylomeDB; Q9NG98; -.
DR BioGRID-ORCS; 35236; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35236; -.
DR PRO; PR:Q9NG98; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0040268; Expressed in egg chamber and 22 other tissues.
DR Genevisible; Q9NG98; DM.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003916; F:DNA topoisomerase activity; IDA:FlyBase.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048589; P:developmental growth; IMP:FlyBase.
DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:FlyBase.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:FlyBase.
DR GO; GO:0042246; P:tissue regeneration; 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; IPR013498; Topo_IA_Znf.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR11390; PTHR11390; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF01396; zf-C4_Topoisom; 1.
DR Pfam; PF06839; zf-GRF; 2.
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; Metal-binding; Reference proteome; Repeat;
KW Topoisomerase; Zinc; Zinc-finger.
FT CHAIN 1..1250
FT /note="DNA topoisomerase 3-alpha"
FT /id="PRO_0000145195"
FT DOMAIN 27..171
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT ZN_FING 1033..1075
FT /note="GRF-type 1"
FT ZN_FING 1150..1192
FT /note="GRF-type 2"
FT REGION 769..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 356
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT CONFLICT 111
FT /note="K -> E (in Ref. 1; AAF71288)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1250 AA; 136137 MW; 108E4AC18EA5677A CRC64;
MKAVLTCFRP VVASHRRYCA NPGQAMKYLN VAEKNDAAKT IAGLLSNGAA QRREGYSVYN
KVFDFEAPVR GQNAKMVMTS VSGHMMQLAF QVSYKNWRTV DPRSLFDAPV KKGVGSDYEP
IKRTLEREVR GCQGLIIWTD CDREGENIGY EIIDVCRAIK PNISVYRATF SEITTVAVRR
ALQQLGQPDK RQSDAVDVRT ELDLRTGAAI TRFQTMRLQR LFPEKIADKL ISYGSCQIPT
LGFVAERYKE IEAFVSEPFW KIKVLHTIDD LTVEFNWARN RLFDKEACEN YLLLCLAEPD
PRALVESVTV KPKHKWRPTP LDTVEMEKLG SRKLKLSAKE TMTIAEKLYT KGFISYPRTE
TNQFSKEFAL APLVEMQTGH RDWGAFAQRV IEWGPNPRNG NKSDQAHPPI HPTKLAENLQ
GNEARVYELV VRHFLACVSK DAVGSETLVH IDIAGEKFTA NGLVIHERNY LDVYVYDKWS
AKQIHHYENG QRFEPTEVSL HEGATTAPPL LTEADLIALM EKHGIGTDAT HAEHINTIKE
RGYIGVLDKG FLVPGVIGMG LYEGYDAMEL ALAKPQLRAE FELDLKLICQ GQKDPKVVLT
EQIAKYKQAY QQITDKITAM DAKISARINE TPAANSAVQE GADGSAPSHG IIQSIFQCPK
CNEAPLALKP KKNQQGWYIG CNNFPDCKNA VWLPTECKDA SVLDECCPTC GDGYRMLKFR
LSTPYYRGVF GTPSGWYKTC LPCDNLFRTT FNINLDSVKK VGGIVGEVRG GGGGPGPGPG
GGGSGRGAGS GGWSSGPGGG GSGGGGGSGG WGSGTGGGGS GGWGSGTGGG GLGGGKGKKP
GGESKKSATK KPPNEPKPKK TKEPKAAPNK KTSSKSSGSI RSFFTSAAPT NSASNGLDEF
FDSNDGFEDA MLAAAESVES SSQPKTISMV PLDDDIAAAF AADDDAEFEA LVNGGTMPTE
SNGDQQLDKS LSEWIKEQDK ADERPMLWGT RERASLGTAA PTPPPKPAAK RPRWDSVERD
STPPSSVPES ETVLCTGCQQ PARQNTVRKN GPNLGRLYYK CPKPDECNFF QWADEPPSSA
KSKNSTGSAP QSTTSWGSNR VVTLPSIQQS NSQRGQSSMR SNSSSTVTIT QTKTKQQERN
TATPGDGEEV MCNCGQLASQ LTVRKDGPNQ GRPFYACPTR EKSCGFFKWG DEDQNQGASS
TSWGSANRNP PGRSQPTAIT SDGPKTRRCG LCRKEGHTRN KCPRKDEFDM