Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P30189 (TOP1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA topoisomerase 1

EC=5.99.1.2
Alternative name(s):
DNA topoisomerase I
Gene names
Name:Top1
ORF Names:CG6146
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length972 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone By similarity.

Catalytic activity

ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.

Subunit structure

Interacts with Topors. Ref.5

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.

Sequence similarities

Belongs to the type IB topoisomerase family.

Ontologies

Keywords
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionIsomerase
Topoisomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from Biological aspect of Ancestor. Source: RefGenome

DNA topological change

Inferred from direct assay PubMed 6294622. Source: FlyBase

cell proliferation

Inferred from mutant phenotype PubMed 10885744. Source: FlyBase

chromatin remodeling

Inferred from Biological aspect of Ancestor. Source: RefGenome

chromosome condensation

Inferred from mutant phenotype PubMed 10885744. Source: FlyBase

chromosome segregation

Inferred from mutant phenotype PubMed 10885744. Source: FlyBase

instar larval development

Inferred from mutant phenotype PubMed 10885744. Source: FlyBase

multicellular organismal development

Inferred from mutant phenotype PubMed 8393572. Source: FlyBase

oogenesis

Inferred from mutant phenotype PubMed 10885744. Source: FlyBase

protein phosphorylation

Inferred from mutant phenotype PubMed 20862310. Source: FlyBase

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 10885744. Source: FlyBase

microtubule associated complex

Inferred from direct assay PubMed 18433294. Source: FlyBase

nuclear euchromatin

Inferred from direct assay PubMed 2819725. Source: FlyBase

nucleolus

Inferred from direct assay PubMed 6095263. Source: FlyBase

nucleus

Inferred from direct assay PubMed 10885744PubMed 6294622PubMed 9632819. Source: FlyBase

polytene chromosome

Inferred from direct assay PubMed 20862310. Source: FlyBase

polytene chromosome puff

Inferred from direct assay PubMed 6095263PubMed 9632819. Source: FlyBase

replication fork protection complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA topoisomerase activity

Inferred from direct assay PubMed 9632819. Source: FlyBase

DNA topoisomerase type I activity

Inferred from direct assay Ref.1PubMed 6294622. Source: FlyBase

DNA topoisomerase type II (ATP-hydrolyzing) activity

Inferred from electronic annotation. Source: InterPro

protein kinase activity

Inferred from direct assay PubMed 20862310. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 972972DNA topoisomerase 1
PRO_0000145205

Regions

Region648 – 6492Interaction with DNA By similarity
Region711 – 7166Interaction with DNA By similarity
Region807 – 8093Interaction with DNA By similarity
Compositional bias32 – 398Poly-His
Compositional bias40 – 198159Ser-rich

Sites

Active site9301O-(3'-phospho-DNA)-tyrosine intermediate By similarity
Site5391Interaction with DNA By similarity
Site5871Interaction with DNA By similarity
Site6351Interaction with DNA By similarity
Site6661Interaction with DNA By similarity
Site7231Interaction with DNA By similarity
Site7541Interaction with DNA By similarity
Site7961Interaction with DNA By similarity
Site8541Interaction with DNA By similarity
Site8721Interaction with DNA By similarity

Amino acid modifications

Modified residue3031Phosphoserine Ref.6
Modified residue3041Phosphotyrosine Ref.6

Experimental info

Sequence conflict401S → H Ref.3
Sequence conflict461S → SSS Ref.3
Sequence conflict2011H → Q in AAF48440. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P30189 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 3764B8BDEEFA30CD

FASTA972111,688
        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 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a gene encoding DNA topoisomerase I in Drosophila melanogaster."
Hsieh T.-S., Brown S.D., Huang P., Fostel J.
Nucleic Acids Res. 20:6177-6182(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation and characterization of a Drosophila gene essential for early embryonic development and formation of cortical cleavage furrows."
Zhang C.X., Lee M.P., Chen A.D., Brown S.D., Hsieh T.-S.
J. Cell Biol. 134:923-934(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Oregon-R.
[3]"The genome sequence of Drosophila melanogaster."
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. expand/collapse author list , 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.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"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."
Secombe J., Parkhurst S.M.
J. Biol. Chem. 279:17126-17133(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOPORS.
[6]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND TYR-304, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74557 mRNA. Translation: AAA28951.1.
U80064 Genomic DNA. Translation: AAC24158.1.
AE014298 Genomic DNA. Translation: AAF48440.1.
PIRS35521.
RefSeqNP_001014742.1. NM_001014742.1.
NP_511161.2. NM_078606.3.
UniGeneDm.2912.

3D structure databases

ProteinModelPortalP30189.
SMRP30189. Positions 426-972.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58813. 4 interactions.
IntActP30189. 1 interaction.
MINTMINT-748832.

Proteomic databases

PaxDbP30189.
PRIDEP30189.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID32458.
KEGGdme:Dmel_CG6146.

Organism-specific databases

CTD7150.
FlyBaseFBgn0004924. Top1.

Phylogenomic databases

eggNOGCOG3569.
InParanoidP30189.
KOK03163.
OrthoDBEOG7CVPX5.
PhylomeDBP30189.

Gene expression databases

BgeeP30189.

Family and domain databases

Gene3D1.10.10.41. 1 hit.
1.10.132.10. 1 hit.
2.170.11.10. 2 hits.
3.90.15.10. 1 hit.
InterProIPR011010. DNA_brk_join_enz.
IPR013034. DNA_topo_domain1.
IPR001631. TopoI.
IPR018521. TopoI_AS.
IPR025834. TopoI_C_dom.
IPR014711. TopoI_cat_a-hlx-sub_euk.
IPR014727. TopoI_cat_a/b-sub_euk.
IPR013500. TopoI_cat_euk.
IPR008336. TopoI_DNA-bd_euk.
IPR013030. TopoI_DNA-bd_mixed-a/b_euk.
IPR013499. TopoI_euk.
[Graphical view]
PfamPF14370. Topo_C_assoc. 1 hit.
PF01028. Topoisom_I. 1 hit.
PF02919. Topoisom_I_N. 1 hit.
[Graphical view]
PRINTSPR00416. EUTPISMRASEI.
SMARTSM00435. TOPEUc. 1 hit.
[Graphical view]
SUPFAMSSF56349. SSF56349. 2 hits.
SSF56741. SSF56741. 1 hit.
PROSITEPS00176. TOPOISOMERASE_I_EUK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTOP1. drosophila.
GenomeRNAi32458.
NextBio778562.
PROP30189.

Entry information

Entry nameTOP1_DROME
AccessionPrimary (citable) accession number: P30189
Secondary accession number(s): Q9VXW6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: July 9, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase