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P30189

- TOP1_DROME

UniProt

P30189 - TOP1_DROME

Protein

DNA topoisomerase 1

Gene

Top1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    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

    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

    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.

    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

    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

    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_001014742.1.
    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

    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 1, 2014
    This is version 128 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