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UniProtKB/Swiss-Prot entry P30189


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TOP1_DROME
Primary accession number P30189
Secondary accession number Q9VXW6
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on April 1, 1993 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 83)
Name and origin of the protein
Protein name DNA topoisomerase 1
Synonyms EC 5.99.1.2
DNA topoisomerase I
Gene name
Name: Top1
ORFNames: CG6146
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/20.23.6177; PubMed=1335568 [NCBI, ExPASy, EBI, Israel, Japan]
Hsieh T.-S., Brown S.D., Huang P., Fostel J.;
"Isolation and characterization of a gene encoding DNA topoisomerase I in Drosophila melanogaster.";
Nucleic Acids Res. 20:6177-6182(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Oregon-R;
DOI=10.1083/jcb.134.4.923; PubMed=8769417 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang C.X., Lee M.P., Chen A.D., Brown S.D., Hsieh T.-S.;
"Isolation and characterization of a Drosophila gene essential for early embryonic development and formation of cortical cleavage furrows.";
J. Cell Biol. 134:923-934(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
INTERACTION WITH TOPORS.
DOI=10.1074/jbc.M310097200; PubMed=14871887 [NCBI, ExPASy, EBI, Israel, Japan]
Secombe J., Parkhurst S.M.;
"Drosophila Topors is a RING finger-containing protein that functions as a ubiquitin-protein isopeptide ligase for the hairy basic helix-loop-helix repressor protein.";
J. Biol. Chem. 279:17126-17133(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND TYR-304, AND MASS SPECTROMETRY.
TISSUE=Embryo;
DOI=10.1021/pr700696a; PubMed=18327897 [NCBI, ExPASy, EBI, Israel, Japan]
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
Comments
  • FUNCTION: The reaction catalyzed by topoisomerases leads to the conversion of one topological isomer of DNA to another.
  • CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
  • SUBUNIT: Interacts with Topors.
  • SUBCELLULAR LOCATION: Nucleus (By similarity).
  • MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.
  • MISCELLANEOUS: When a topoisomerase transiently breaks a DNA backbone bond, it simultaneously forms a protein-DNA link, in which a tyrosyl oxygen in the enzyme is joined to a DNA phosphorus at one end of the enzyme-severed DNA strand.
  • SIMILARITY: Belongs to the eukaryotic type I topoisomerase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M74557; AAA28951.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U80064; AAC24158.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014298; AAF48440.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S35521; S35521.
RefSeq NP_511161.2; -.
UniGene Dm.2912
3D structure databases
HSSP P11387; 1A35. [HSSP ENTRY / PDB]
SMR P30189; 426-972.
ModBase P30189.
Protein-protein interaction databases
IntAct P30189; 1.
Organism-specific databases
FlyBase FBgn0004924; Top1.
Gene expression databases
ArrayExpress P30189; -.
GermOnline CG6146; Drosophila melanogaster.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from FlyBase).
GO:0005730; Cellular component: nucleolus (inferred from direct assay from FlyBase).
GO:0005703; Cellular component: polytene chromosome puff (inferred from direct assay from FlyBase).
GO:0003918; Molecular function: DNA topoisomerase (ATP-hydrolyzing) activity (inferred from electronic annotation from InterPro).
GO:0003917; Molecular function: DNA topoisomerase type I activity (inferred from electronic annotation from InterPro).
GO:0008283; Biological process: cell proliferation (inferred from mutant phenotype from FlyBase).
GO:0030261; Biological process: chromosome condensation (inferred from mutant phenotype from FlyBase).
GO:0007059; Biological process: chromosome segregation (inferred from mutant phenotype from FlyBase).
GO:0006265; Biological process: DNA topological change (inferred from electronic annotation from InterPro).
GO:0006268; Biological process: DNA unwinding during replication (inferred from electronic annotation from InterPro).
GO:0009790; Biological process: embryonic development (inferred from mutant phenotype from FlyBase).
GO:0002168; Biological process: instar larval development (inferred from mutant phenotype from FlyBase).
GO:0048477; Biological process: oogenesis (inferred from mutant phenotype from FlyBase).
QuickGo view.
Family and domain databases
InterPro IPR001631; TopoI_C.
IPR013499; TopoI_C_euk.
IPR014711; TopoI_cat_a-hlx-sub_euk.
IPR014727; TopoI_cat_a/b-sub_euk.
IPR013500; TopoI_cat_euk.
IPR013030; TopoI_DNA-bd_mixed-a/b_euk.
IPR008336; TopoI_DNA_bd_euk.
Graphical view of domain structure.
Gene3D G3DSA:3.90.15.10; TopoI_cat_a-hlx-sub_euk; 1.
G3DSA:1.10.132.10; TopoI_cat_a/b-sub_euk; 1.
G3DSA:2.170.11.10; TopoI_DNA-bd_mixed-a/b_euk; 1.
Pfam PF01028; Topoisom_I; 1.
PF02919; Topoisom_I_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00416; EUTPISMRASEI.
SMART SM00435; TOPEUc; 1.
SMART graphical view of domain structure.
PROSITE PS00176; TOPOISOMERASE_I_EUK; 1.
Genome annotation databases
Ensembl CG6146; Drosophila melanogaster. [Contig view]
GeneID 32458; -.
Other
NextBio 778562; -.
ProtoNet P30189.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; DNA-binding; Isomerase; Nucleus; Phosphoprotein; Topoisomerase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   972  972     DNA topoisomerase 1. PRO_0000145205
COMPBIAS   32    39  8     Poly-His. 
COMPBIAS   40   198  159     Ser-rich. 
ACT_SITE   930   930        O-(3'-phospho-DNA)-tyrosine intermediate (By similarity). 
MOD_RES   303   303        Phosphoserine. 
MOD_RES   304   304        Phosphotyrosine. 
CONFLICT   40    40        S -> H (in Ref. 3). 
CONFLICT   46    46        S -> SSS (in Ref. 3). 
CONFLICT   201   201        H -> Q (in Ref. 3; AAF48440). 
Sequence information
Length: 972 AA [This is the length of the unprocessed precursor] Molecular weight: 111688 Da [This is the MW of the unprocessed precursor] CRC64: 3764B8BDEEFA30CD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSGDVAAENS IHIQNGGSCE VVQSNGVTTN GHGHHHHHHS SSSSSSKHKS SSKDKHRDRE 

        70         80         90        100        110        120 
REHKSSNSSS SSKEHKSSSR DKDRHKSSSS SSKHRDKDKE RDGSSNSHRS GSSSSHKDKD 

       130        140        150        160        170        180 
GSSSSKHKSS SGHHKRSSKD KERRDKDKDR GSSSSSRHKS SSSSRDKERS SSSHKSSSSS 

       190        200        210        220        230        240 
SSSKSKHSSS RHSSSSSSKD HPSYDGVFVK PEPVSQQLMH SGSVDAFQMQ QLGSYEAAAA 

       250        260        270        280        290        300 
GTNFNGNGNV AGANYKNGYE ESIVDIKKEE ESFNNLSQAS SCDYSMSQFR ADEPPFVVKH 

       310        320        330        340        350        360 
EQSYAEEDST MNYNDHDDDA DEMNDDEEDV PLAMRKRKQE ATDRPDGGMD NDDDDDIPLL 

       370        380        390        400        410        420 
ARKKVKKEKI KKESKEKSKK RVKEEPSDDY GNVKPKKKKM KKEPEPAVSP GKRQKAKAKV 

       430        440        450        460        470        480 
EEEEVWRWWE EEKRADGVKW STLEHKGPVF APRYERVPRN VRFYYDGKPL ELSEETEEAA 

       490        500        510        520        530        540 
TFYAKMLNHD YCTKEVFNNN FFKDFRKSMT PREREIIKDF RKCNFQEMFN YFQAESEKRK 

       550        560        570        580        590        600 
AASKEEKLIK KNENEALMKE FGFCMIDGHK EKIGNFRLEP PGLFRGRGEH PKMGMIKRRI 

       610        620        630        640        650        660 
QASDVSINCG KDSKVPSPPP GSRWKEVRHD NTVTWLASWI ENVQGQVKYI MLNPSSKLKG 

       670        680        690        700        710        720 
EKDHIKYETA RRLDKVIDKI RATYRDEWKS KEMRVRQRAV ALYFIDKLAL RAGNEKDEDQ 

       730        740        750        760        770        780 
ADTVGCCSLR VEHVQLHKEL NGKENVVVFD FPGKDSIRYY NEVEVEKRVF KNLELFMEHK 

       790        800        810        820        830        840 
KEGDDLFDRL NTQVLNEHLK ELMEGLTAKV FRTYNASKTL QSQLDLLTDP SATVPEKLLA 

       850        860        870        880        890        900 
YNRANRAVAI LCNHQRSVPK SHEKSMENLK EKIKAKREAI EKCESEYHSR DEKKGKQLER 

       910        920        930        940        950        960 
LRDQLKKLEL QETDRDENKT IALGTSKLNY LDPRISVAWC KKHDVPIEKI FNKTQRTKFL 

       970 
WAVHMADENY RF 

P30189 in FASTA format

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