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P30189

- TOP1_DROME

UniProt

P30189 - TOP1_DROME

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Protein
DNA topoisomerase 1
Gene
Top1, CG6146
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei539 – 5391Interaction with DNA By similarity
Sitei587 – 5871Interaction with DNA By similarity
Sitei635 – 6351Interaction with DNA By similarity
Sitei666 – 6661Interaction with DNA By similarity
Sitei723 – 7231Interaction with DNA By similarity
Sitei754 – 7541Interaction with DNA By similarity
Sitei796 – 7961Interaction with DNA By similarity
Sitei854 – 8541Interaction with DNA By similarity
Sitei872 – 8721Interaction with DNA By similarity
Active sitei930 – 9301O-(3'-phospho-DNA)-tyrosine intermediate By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. DNA topoisomerase activity Source: FlyBase
  4. DNA topoisomerase type I activity Source: FlyBase
  5. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: InterPro
  6. protein kinase activity Source: FlyBase

GO - Biological processi

  1. DNA replication Source: RefGenome
  2. DNA topological change Source: FlyBase
  3. cell proliferation Source: FlyBase
  4. chromatin remodeling Source: RefGenome
  5. chromosome condensation Source: FlyBase
  6. chromosome segregation Source: FlyBase
  7. instar larval development Source: FlyBase
  8. multicellular organismal development Source: FlyBase
  9. oogenesis Source: FlyBase
  10. protein phosphorylation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Topoisomerase

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA topoisomerase 1 (EC:5.99.1.2)
Alternative name(s):
DNA topoisomerase I
Gene namesi
Name:Top1
ORF Names:CG6146
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0004924. Top1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. microtubule associated complex Source: FlyBase
  3. nuclear euchromatin Source: FlyBase
  4. nucleolus Source: FlyBase
  5. nucleus Source: FlyBase
  6. polytene chromosome Source: FlyBase
  7. polytene chromosome puff Source: FlyBase
  8. replication fork protection complex Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 972972DNA topoisomerase 1
PRO_0000145205Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei303 – 3031Phosphoserine1 Publication
Modified residuei304 – 3041Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP30189.
PRIDEiP30189.

Expressioni

Gene expression databases

BgeeiP30189.

Interactioni

Subunit structurei

Interacts with Topors.1 Publication

Protein-protein interaction databases

BioGridi58813. 4 interactions.
IntActiP30189. 1 interaction.
MINTiMINT-748832.

Structurei

3D structure databases

ProteinModelPortaliP30189.
SMRiP30189. Positions 426-972.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni648 – 6492Interaction with DNA By similarity
Regioni711 – 7166Interaction with DNA By similarity
Regioni807 – 8093Interaction with DNA By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi32 – 398Poly-His
Compositional biasi40 – 198159Ser-rich
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3569.
InParanoidiP30189.
KOiK03163.
OrthoDBiEOG7CVPX5.
PhylomeDBiP30189.

Family and domain databases

Gene3Di1.10.10.41. 1 hit.
1.10.132.10. 1 hit.
2.170.11.10. 2 hits.
3.90.15.10. 1 hit.
InterProiIPR011010. 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]
PfamiPF14370. Topo_C_assoc. 1 hit.
PF01028. Topoisom_I. 1 hit.
PF02919. Topoisom_I_N. 1 hit.
[Graphical view]
PRINTSiPR00416. EUTPISMRASEI.
SMARTiSM00435. TOPEUc. 1 hit.
[Graphical view]
SUPFAMiSSF56349. SSF56349. 2 hits.
SSF56741. SSF56741. 1 hit.
PROSITEiPS00176. TOPOISOMERASE_I_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30189-1 [UniParc]FASTAAdd to Basket

« Hide

MSGDVAAENS IHIQNGGSCE VVQSNGVTTN GHGHHHHHHS SSSSSSKHKS    50
SSKDKHRDRE REHKSSNSSS SSKEHKSSSR DKDRHKSSSS SSKHRDKDKE 100
RDGSSNSHRS GSSSSHKDKD GSSSSKHKSS SGHHKRSSKD KERRDKDKDR 150
GSSSSSRHKS SSSSRDKERS SSSHKSSSSS SSSKSKHSSS RHSSSSSSKD 200
HPSYDGVFVK PEPVSQQLMH SGSVDAFQMQ QLGSYEAAAA GTNFNGNGNV 250
AGANYKNGYE ESIVDIKKEE ESFNNLSQAS SCDYSMSQFR ADEPPFVVKH 300
EQSYAEEDST MNYNDHDDDA DEMNDDEEDV PLAMRKRKQE ATDRPDGGMD 350
NDDDDDIPLL ARKKVKKEKI KKESKEKSKK RVKEEPSDDY GNVKPKKKKM 400
KKEPEPAVSP GKRQKAKAKV EEEEVWRWWE EEKRADGVKW STLEHKGPVF 450
APRYERVPRN VRFYYDGKPL ELSEETEEAA TFYAKMLNHD YCTKEVFNNN 500
FFKDFRKSMT PREREIIKDF RKCNFQEMFN YFQAESEKRK AASKEEKLIK 550
KNENEALMKE FGFCMIDGHK EKIGNFRLEP PGLFRGRGEH PKMGMIKRRI 600
QASDVSINCG KDSKVPSPPP GSRWKEVRHD NTVTWLASWI ENVQGQVKYI 650
MLNPSSKLKG EKDHIKYETA RRLDKVIDKI RATYRDEWKS KEMRVRQRAV 700
ALYFIDKLAL RAGNEKDEDQ ADTVGCCSLR VEHVQLHKEL NGKENVVVFD 750
FPGKDSIRYY NEVEVEKRVF KNLELFMEHK KEGDDLFDRL NTQVLNEHLK 800
ELMEGLTAKV FRTYNASKTL QSQLDLLTDP SATVPEKLLA YNRANRAVAI 850
LCNHQRSVPK SHEKSMENLK EKIKAKREAI EKCESEYHSR DEKKGKQLER 900
LRDQLKKLEL QETDRDENKT IALGTSKLNY LDPRISVAWC KKHDVPIEKI 950
FNKTQRTKFL WAVHMADENY RF 972
Length:972
Mass (Da):111,688
Last modified:April 1, 1993 - v1
Checksum:i3764B8BDEEFA30CD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401S → H1 Publication
Sequence conflicti46 – 461S → SSS1 Publication
Sequence conflicti201 – 2011H → Q in AAF48440. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M74557 mRNA. Translation: AAA28951.1.
U80064 Genomic DNA. Translation: AAC24158.1.
AE014298 Genomic DNA. Translation: AAF48440.1.
PIRiS35521.
RefSeqiNP_001014742.1. NM_001014742.1.
NP_511161.2. NM_078606.3.
UniGeneiDm.2912.

Genome annotation databases

GeneIDi32458.
KEGGidme:Dmel_CG6146.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M74557 mRNA. Translation: AAA28951.1 .
U80064 Genomic DNA. Translation: AAC24158.1 .
AE014298 Genomic DNA. Translation: AAF48440.1 .
PIRi S35521.
RefSeqi NP_001014742.1. NM_001014742.1.
NP_511161.2. NM_078606.3.
UniGenei Dm.2912.

3D structure databases

ProteinModelPortali P30189.
SMRi P30189. Positions 426-972.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 58813. 4 interactions.
IntActi P30189. 1 interaction.
MINTi MINT-748832.

Proteomic databases

PaxDbi P30189.
PRIDEi P30189.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 32458.
KEGGi dme:Dmel_CG6146.

Organism-specific databases

CTDi 7150.
FlyBasei FBgn0004924. Top1.

Phylogenomic databases

eggNOGi COG3569.
InParanoidi P30189.
KOi K03163.
OrthoDBi EOG7CVPX5.
PhylomeDBi P30189.

Miscellaneous databases

ChiTaRSi TOP1. drosophila.
GenomeRNAii 32458.
NextBioi 778562.
PROi P30189.

Gene expression databases

Bgeei P30189.

Family and domain databases

Gene3Di 1.10.10.41. 1 hit.
1.10.132.10. 1 hit.
2.170.11.10. 2 hits.
3.90.15.10. 1 hit.
InterProi IPR011010. 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 ]
Pfami PF14370. Topo_C_assoc. 1 hit.
PF01028. Topoisom_I. 1 hit.
PF02919. Topoisom_I_N. 1 hit.
[Graphical view ]
PRINTSi PR00416. EUTPISMRASEI.
SMARTi SM00435. TOPEUc. 1 hit.
[Graphical view ]
SUPFAMi SSF56349. SSF56349. 2 hits.
SSF56741. SSF56741. 1 hit.
PROSITEi PS00176. TOPOISOMERASE_I_EUK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiTOP1_DROME
AccessioniPrimary (citable) accession number: P30189
Secondary accession number(s): Q9VXW6
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi