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P30189

- TOP1_DROME

UniProt

P30189 - TOP1_DROME

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Protein

DNA topoisomerase 1

Gene

Top1

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).By similarity

Catalytic activityi

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

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. cell proliferation Source: FlyBase
  2. chromatin remodeling Source: RefGenome
  3. chromosome condensation Source: FlyBase
  4. chromosome segregation Source: FlyBase
  5. DNA replication Source: RefGenome
  6. DNA topological change 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 1PRO_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.
ExpressionAtlasiP30189. differential.

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Compositional bias

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

Sequence similaritiesi

Belongs to the type IB topoisomerase family.Curated

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

        10         20         30         40         50
MSGDVAAENS IHIQNGGSCE VVQSNGVTTN GHGHHHHHHS SSSSSSKHKS
60 70 80 90 100
SSKDKHRDRE REHKSSNSSS SSKEHKSSSR DKDRHKSSSS SSKHRDKDKE
110 120 130 140 150
RDGSSNSHRS GSSSSHKDKD GSSSSKHKSS SGHHKRSSKD KERRDKDKDR
160 170 180 190 200
GSSSSSRHKS SSSSRDKERS SSSHKSSSSS SSSKSKHSSS RHSSSSSSKD
210 220 230 240 250
HPSYDGVFVK PEPVSQQLMH SGSVDAFQMQ QLGSYEAAAA GTNFNGNGNV
260 270 280 290 300
AGANYKNGYE ESIVDIKKEE ESFNNLSQAS SCDYSMSQFR ADEPPFVVKH
310 320 330 340 350
EQSYAEEDST MNYNDHDDDA DEMNDDEEDV PLAMRKRKQE ATDRPDGGMD
360 370 380 390 400
NDDDDDIPLL ARKKVKKEKI KKESKEKSKK RVKEEPSDDY GNVKPKKKKM
410 420 430 440 450
KKEPEPAVSP GKRQKAKAKV EEEEVWRWWE EEKRADGVKW STLEHKGPVF
460 470 480 490 500
APRYERVPRN VRFYYDGKPL ELSEETEEAA TFYAKMLNHD YCTKEVFNNN
510 520 530 540 550
FFKDFRKSMT PREREIIKDF RKCNFQEMFN YFQAESEKRK AASKEEKLIK
560 570 580 590 600
KNENEALMKE FGFCMIDGHK EKIGNFRLEP PGLFRGRGEH PKMGMIKRRI
610 620 630 640 650
QASDVSINCG KDSKVPSPPP GSRWKEVRHD NTVTWLASWI ENVQGQVKYI
660 670 680 690 700
MLNPSSKLKG EKDHIKYETA RRLDKVIDKI RATYRDEWKS KEMRVRQRAV
710 720 730 740 750
ALYFIDKLAL RAGNEKDEDQ ADTVGCCSLR VEHVQLHKEL NGKENVVVFD
760 770 780 790 800
FPGKDSIRYY NEVEVEKRVF KNLELFMEHK KEGDDLFDRL NTQVLNEHLK
810 820 830 840 850
ELMEGLTAKV FRTYNASKTL QSQLDLLTDP SATVPEKLLA YNRANRAVAI
860 870 880 890 900
LCNHQRSVPK SHEKSMENLK EKIKAKREAI EKCESEYHSR DEKKGKQLER
910 920 930 940 950
LRDQLKKLEL QETDRDENKT IALGTSKLNY LDPRISVAWC KKHDVPIEKI
960 970
FNKTQRTKFL WAVHMADENY RF
Length:972
Mass (Da):111,688
Last modified:April 1, 1993 - v1
Checksum:i3764B8BDEEFA30CD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401S → H(PubMed:10731132)Curated
Sequence conflicti46 – 461S → SSS(PubMed:10731132)Curated
Sequence conflicti201 – 2011H → Q in AAF48440. (PubMed:10731132)Curated

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_001014742.2.
NP_511161.2. NM_078606.4.
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_001014742.2.
NP_511161.2. NM_078606.4.
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.
ExpressionAtlasi P30189. differential.

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: October 29, 2014
This is version 129 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