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P07799

- TOP1_SCHPO

UniProt

P07799 - TOP1_SCHPO

Protein

DNA topoisomerase 1

Gene

top1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (27 Apr 2001)
      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
    Sitei343 – 3431Interaction with DNABy similarity
    Sitei391 – 3911Interaction with DNABy similarity
    Sitei422 – 4221Interaction with DNABy similarity
    Sitei479 – 4791Interaction with DNABy similarity
    Sitei505 – 5051Interaction with DNABy similarity
    Sitei548 – 5481Interaction with DNABy similarity
    Sitei605 – 6051Interaction with DNABy similarity
    Active sitei773 – 7731O-(3'-phospho-DNA)-tyrosine intermediate1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. DNA binding Source: PomBase
    2. DNA topoisomerase type I activity Source: PomBase
    3. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: InterPro

    GO - Biological processi

    1. chromatin assembly or disassembly Source: PomBase
    2. chromatin organization Source: PomBase
    3. DNA topological change Source: PomBase
    4. mitotic chromosome condensation Source: PomBase
    5. transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: PomBase

    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:SPBC1703.14c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC1703.14c.

    Subcellular locationi

    GO - Cellular componenti

    1. nuclear chromatin Source: PomBase
    2. nucleolus Source: PomBase
    3. nucleus Source: PomBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 814814DNA topoisomerase 1PRO_0000145209Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei52 – 521Phosphoserine1 Publication
    Modified residuei54 – 541Phosphoserine1 Publication
    Modified residuei136 – 1361Phosphoserine1 Publication
    Modified residuei138 – 1381Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP07799.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi276575. 81 interactions.
    MINTiMINT-4686963.
    STRINGi4896.SPBC1703.14c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliP07799.
    SMRiP07799. Positions 180-608, 762-807.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni404 – 4052Interaction with DNABy similarity
    Regioni467 – 4726Interaction with DNABy similarity
    Regioni559 – 5613Interaction with DNABy similarity

    Sequence similaritiesi

    Belongs to the type IB topoisomerase family.Curated

    Phylogenomic databases

    eggNOGiCOG3569.
    HOGENOMiHOG000105469.
    KOiK03163.
    OMAiKSVDEDW.
    OrthoDBiEOG7966R0.
    PhylomeDBiP07799.

    Family and domain databases

    Gene3Di1.10.10.41. 1 hit.
    1.10.132.10. 2 hits.
    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.

    P07799-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSDSDSVS LSIRRRQRRG SSKRISMKES DEESDSSENH PLSESLNKKS    50
    KSESDEDDIP IRKRRASSKK NMSNSSSKKR AKVMGNGGLK NGKKTAVVKE 100
    EEDFNEIAKP SPKHKRVSKA NGSKNGAKSA VKKEESDTDD SVPLRAVSTV 150
    SLTPYKSELP SGASTTQNRS PNDEEDEDED YKWWTSENID DTQKWTTLEH 200
    NGVIFAPPYE PLPKNVKLIY DGNPVNLPPE AEEVAGFYAA MLETDHAKNP 250
    VFQDNFFRDF LKVCDECNFN HNIKEFSKCD FTQMFHHFEQ KREEKKSMPK 300
    EQKKAIKQKK DEEEEKYKWC ILDGRKEKVG NFRIEPPGLF RGRGSHPKTG 350
    SLKRRVYPEQ ITINIGEGVP VPEPLPGHQW AEVKHDNTVT WLATWHENIN 400
    NNVKYVFLAA GSSLKGQSDL KKYEKSRKLK DYIDDIRKGY RKDLKSELTV 450
    ERQRGTAMYL IDVFALRAGN EKGEDEADTV GCCSLRYEHV TLKPPRTVVF 500
    DFLGKDSIRY YNEVEVDPQV FKNLKIFKRP PKKEGDLIFD RLSTNSLNKY 550
    LTSLMDGLSA KVFRTYNASY TMAEELKKMP KNLTLADKIL FYNRANRTVA 600
    ILCNHQRSVT KNHDVQMERF AERIKALQYQ RMRLRKMMLN LEPKLAKSKP 650
    ELLAKEEGIT DSWIVKHHET LYELEKEKIK KKFDRENEKL AAEDPKSVLP 700
    ESELEVRLKA ADELKKALDA ELKSKKVDPG RSSMEQLEKR LNKLNERINV 750
    MRTQMIDKDE NKTTALGTSK INYIDPRLTY SFSKREDVPI EKLFSKTIRD 800
    KFNWAADTPP DWKW 814
    Length:814
    Mass (Da):93,981
    Last modified:April 27, 2001 - v2
    Checksum:i842D8D81C92CB0A3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 82Missing(PubMed:2827111)Curated
    Sequence conflicti308 – 3081Q → E in CAA29559. (PubMed:2827111)Curated
    Sequence conflicti446 – 4461S → N in CAA29559. (PubMed:2827111)Curated
    Sequence conflicti698 – 6981V → M in CAA29559. (PubMed:2827111)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06201 Genomic DNA. Translation: CAA29559.1.
    CU329671 Genomic DNA. Translation: CAB66458.1.
    PIRiS03329. ISZPT1.
    T50327.
    RefSeqiNP_596209.1. NM_001022128.2.

    Genome annotation databases

    EnsemblFungiiSPBC1703.14c.1; SPBC1703.14c.1:pep; SPBC1703.14c.
    GeneIDi2540032.
    KEGGispo:SPBC1703.14c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06201 Genomic DNA. Translation: CAA29559.1 .
    CU329671 Genomic DNA. Translation: CAB66458.1 .
    PIRi S03329. ISZPT1.
    T50327.
    RefSeqi NP_596209.1. NM_001022128.2.

    3D structure databases

    ProteinModelPortali P07799.
    SMRi P07799. Positions 180-608, 762-807.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 276575. 81 interactions.
    MINTi MINT-4686963.
    STRINGi 4896.SPBC1703.14c-1.

    Proteomic databases

    MaxQBi P07799.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC1703.14c.1 ; SPBC1703.14c.1:pep ; SPBC1703.14c .
    GeneIDi 2540032.
    KEGGi spo:SPBC1703.14c.

    Organism-specific databases

    PomBasei SPBC1703.14c.

    Phylogenomic databases

    eggNOGi COG3569.
    HOGENOMi HOG000105469.
    KOi K03163.
    OMAi KSVDEDW.
    OrthoDBi EOG7966R0.
    PhylomeDBi P07799.

    Miscellaneous databases

    NextBioi 20801174.

    Family and domain databases

    Gene3Di 1.10.10.41. 1 hit.
    1.10.132.10. 2 hits.
    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. "Cloning and sequencing of Schizosaccharomyces pombe DNA topoisomerase I gene, and effect of gene disruption."
      Uemura T., Morino K., Uzawa S., Shiozaki K., Yanagida M.
      Nucleic Acids Res. 15:9727-9739(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    3. "Mapping of the active site tyrosine of eukaryotic DNA topoisomerase I."
      Eng W.-K., Pandit S.D., Sternglanz R.
      J. Biol. Chem. 264:13373-13376(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE TYR-773.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-54; SER-136 AND THR-138, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiTOP1_SCHPO
    AccessioniPrimary (citable) accession number: P07799
    Secondary accession number(s): Q9P7V7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    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. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3