ID   TOP1_DROME              Reviewed;         972 AA.
AC   P30189; Q9VXW6;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   16-JUN-2009, entry version 86.
DE   RecName: Full=DNA topoisomerase 1;
DE            EC=5.99.1.2;
DE   AltName: Full=DNA topoisomerase I;
GN   Name=Top1; ORFNames=CG6146;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93117086; PubMed=1335568; DOI=10.1093/nar/20.23.6177;
RA   Hsieh T.-S., Brown S.D., Huang P., Fostel J.;
RT   "Isolation and characterization of a gene encoding DNA topoisomerase I
RT   in Drosophila melanogaster.";
RL   Nucleic Acids Res. 20:6177-6182(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Oregon-R;
RX   MEDLINE=96354910; PubMed=8769417; DOI=10.1083/jcb.134.4.923;
RA   Zhang C.X., Lee M.P., Chen A.D., Brown S.D., Hsieh T.-S.;
RT   "Isolation and characterization of a Drosophila gene essential for
RT   early embryonic development and formation of cortical cleavage
RT   furrows.";
RL   J. Cell Biol. 134:923-934(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=20196006; 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RX   MEDLINE=22426069; PubMed=12537572;
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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   INTERACTION WITH TOPORS.
RX   PubMed=14871887; DOI=10.1074/jbc.M310097200;
RA   Secombe J., Parkhurst S.M.;
RT   "Drosophila Topors is a RING finger-containing protein that functions
RT   as a ubiquitin-protein isopeptide ligase for the hairy basic helix-
RT   loop-helix repressor protein.";
RL   J. Biol. Chem. 279:17126-17133(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND TYR-304, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: The reaction catalyzed by topoisomerases leads to the
CC       conversion of one topological isomer of DNA to another.
CC   -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded
CC       DNA, followed by passage and rejoining.
CC   -!- SUBUNIT: Interacts with Topors.
CC   -!- INTERACTION:
CC       Q9V8P9:Topors; NbExp=1; IntAct=EBI-108030, EBI-147805;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC       negative and positive supercoils, whereas prokaryotic enzymes
CC       relax only negative supercoils.
CC   -!- MISCELLANEOUS: When a topoisomerase transiently breaks a DNA
CC       backbone bond, it simultaneously forms a protein-DNA link, in
CC       which a tyrosyl oxygen in the enzyme is joined to a DNA phosphorus
CC       at one end of the enzyme-severed DNA strand.
CC   -!- SIMILARITY: Belongs to the eukaryotic type I topoisomerase family.
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DR   EMBL; M74557; AAA28951.1; -; mRNA.
DR   EMBL; U80064; AAC24158.1; -; Genomic_DNA.
DR   EMBL; AE014298; AAF48440.1; -; Genomic_DNA.
DR   PIR; S35521; S35521.
DR   RefSeq; NP_511161.2; -.
DR   UniGene; Dm.2912; -.
DR   HSSP; P11387; 1A35.
DR   SMR; P30189; 426-972.
DR   IntAct; P30189; 1.
DR   PRIDE; P30189; -.
DR   Ensembl; FBgn0004924; Drosophila melanogaster.
DR   GeneID; 32458; -.
DR   FlyBase; FBgn0004924; Top1.
DR   BRENDA; 5.99.1.2; 48.
DR   NextBio; 778562; -.
DR   ArrayExpress; P30189; -.
DR   GermOnline; CG6146; Drosophila melanogaster.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR   GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0003917; F:DNA topoisomerase type I activity; IDA:FlyBase.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008283; P:cell proliferation; IMP:FlyBase.
DR   GO; GO:0030261; P:chromosome condensation; IMP:FlyBase.
DR   GO; GO:0007059; P:chromosome segregation; IMP:FlyBase.
DR   GO; GO:0006265; P:DNA topological change; IDA:FlyBase.
DR   GO; GO:0006268; P:DNA unwinding during replication; IEA:InterPro.
DR   GO; GO:0009790; P:embryonic development; IMP:FlyBase.
DR   GO; GO:0002168; P:instar larval development; IMP:FlyBase.
DR   GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR   InterPro; IPR018521; TopoI_AS.
DR   InterPro; IPR001631; TopoI_C.
DR   InterPro; IPR013499; TopoI_C_euk.
DR   InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR   InterPro; IPR014727; TopoI_cat_a/b-sub_euk.
DR   InterPro; IPR013500; TopoI_cat_euk.
DR   InterPro; IPR013030; TopoI_DNA-bd_mixed-a/b_euk.
DR   InterPro; IPR008336; TopoI_DNA_bd_euk.
DR   Gene3D; G3DSA:3.90.15.10; TopoI_cat_a-hlx-sub_euk; 1.
DR   Gene3D; G3DSA:1.10.132.10; TopoI_cat_a/b-sub_euk; 1.
DR   Gene3D; G3DSA:2.170.11.10; TopoI_DNA-bd_mixed-a/b_euk; 1.
DR   Pfam; PF01028; Topoisom_I; 1.
DR   Pfam; PF02919; Topoisom_I_N; 1.
DR   PRINTS; PR00416; EUTPISMRASEI.
DR   SMART; SM00435; TOPEUc; 1.
DR   PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; DNA-binding; Isomerase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Topoisomerase.
FT   CHAIN         1    972       DNA topoisomerase 1.
FT                                /FTId=PRO_0000145205.
FT   COMPBIAS     32     39       Poly-His.
FT   COMPBIAS     40    198       Ser-rich.
FT   ACT_SITE    930    930       O-(3'-phospho-DNA)-tyrosine intermediate
FT                                (By similarity).
FT   MOD_RES     303    303       Phosphoserine.
FT   MOD_RES     304    304       Phosphotyrosine.
FT   CONFLICT     40     40       S -> H (in Ref. 3).
FT   CONFLICT     46     46       S -> SSS (in Ref. 3).
FT   CONFLICT    201    201       H -> Q (in Ref. 3; AAF48440).
SQ   SEQUENCE   972 AA;  111688 MW;  3764B8BDEEFA30CD CRC64;
     MSGDVAAENS IHIQNGGSCE VVQSNGVTTN GHGHHHHHHS SSSSSSKHKS SSKDKHRDRE
     REHKSSNSSS SSKEHKSSSR DKDRHKSSSS SSKHRDKDKE RDGSSNSHRS GSSSSHKDKD
     GSSSSKHKSS SGHHKRSSKD KERRDKDKDR GSSSSSRHKS SSSSRDKERS SSSHKSSSSS
     SSSKSKHSSS RHSSSSSSKD HPSYDGVFVK PEPVSQQLMH SGSVDAFQMQ QLGSYEAAAA
     GTNFNGNGNV AGANYKNGYE ESIVDIKKEE ESFNNLSQAS SCDYSMSQFR ADEPPFVVKH
     EQSYAEEDST MNYNDHDDDA DEMNDDEEDV PLAMRKRKQE ATDRPDGGMD NDDDDDIPLL
     ARKKVKKEKI KKESKEKSKK RVKEEPSDDY GNVKPKKKKM KKEPEPAVSP GKRQKAKAKV
     EEEEVWRWWE EEKRADGVKW STLEHKGPVF APRYERVPRN VRFYYDGKPL ELSEETEEAA
     TFYAKMLNHD YCTKEVFNNN FFKDFRKSMT PREREIIKDF RKCNFQEMFN YFQAESEKRK
     AASKEEKLIK KNENEALMKE FGFCMIDGHK EKIGNFRLEP PGLFRGRGEH PKMGMIKRRI
     QASDVSINCG KDSKVPSPPP GSRWKEVRHD NTVTWLASWI ENVQGQVKYI MLNPSSKLKG
     EKDHIKYETA RRLDKVIDKI RATYRDEWKS KEMRVRQRAV ALYFIDKLAL RAGNEKDEDQ
     ADTVGCCSLR VEHVQLHKEL NGKENVVVFD FPGKDSIRYY NEVEVEKRVF KNLELFMEHK
     KEGDDLFDRL NTQVLNEHLK ELMEGLTAKV FRTYNASKTL QSQLDLLTDP SATVPEKLLA
     YNRANRAVAI LCNHQRSVPK SHEKSMENLK EKIKAKREAI EKCESEYHSR DEKKGKQLER
     LRDQLKKLEL QETDRDENKT IALGTSKLNY LDPRISVAWC KKHDVPIEKI FNKTQRTKFL
     WAVHMADENY RF
//