(data stored in ACNUC7421 zone)

SWISSPROT: A2Q8K2_ASPNC

ID   A2Q8K2_ASPNC            Unreviewed;       884 AA.
AC   A2Q8K2;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 85.
DE   RecName: Full=DNA topoisomerase I {ECO:0000256|RuleBase:RU365101};
DE            EC=5.6.2.1 {ECO:0000256|RuleBase:RU365101};
DE   AltName: Full=DNA topoisomerase 1 {ECO:0000256|RuleBase:RU365101};
GN   ORFNames=An01g04640 {ECO:0000313|EMBL:CAK36999.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK36999.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Releases the supercoiling and torsional tension of DNA
CC       introduced during the DNA replication and transcription by transiently
CC       cleaving and rejoining one strand of the DNA duplex. Introduces a
CC       single-strand break via transesterification at the specific target site
CC       5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is
CC       attacked by the catalytic tyrosine of the enzyme, resulting in the
CC       formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the
CC       expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes
CC       passage around the unbroken strand thus removing DNA supercoils.
CC       Finally, in the religation step, the DNA 5'-OH attacks the covalent
CC       intermediate to expel the active-site tyrosine and restore the DNA
CC       phosphodiester backbone. {ECO:0000256|RuleBase:RU365101}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC         passage and rejoining.; EC=5.6.2.1;
CC         Evidence={ECO:0000256|RuleBase:RU365101};
CC   -!- SIMILARITY: Belongs to the type IB topoisomerase family.
CC       {ECO:0000256|RuleBase:RU365101}.
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DR   EMBL; AM269963; CAK36999.1; -; Genomic_DNA.
DR   RefSeq; XP_001388891.1; XM_001388854.2.
DR   PaxDb; A2Q8K2; -.
DR   EnsemblFungi; CAK36999; CAK36999; An01g04640.
DR   GeneID; 4978442; -.
DR   KEGG; ang:ANI_1_596014; -.
DR   HOGENOM; HOG000105469; -.
DR   KO; K03163; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd00659; Topo_IB_C; 1.
DR   Gene3D; 1.10.10.41; -; 1.
DR   Gene3D; 1.10.132.10; -; 2.
DR   Gene3D; 2.170.11.10; -; 1.
DR   Gene3D; 3.90.15.10; -; 1.
DR   InterPro; IPR011010; DNA_brk_join_enz.
DR   InterPro; IPR013034; DNA_topo_DNA_db_N_dom1.
DR   InterPro; IPR013030; DNA_topo_DNA_db_N_dom2.
DR   InterPro; IPR001631; TopoI.
DR   InterPro; IPR018521; TopoI_AS.
DR   InterPro; IPR025834; TopoI_C_dom.
DR   InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR   InterPro; IPR014727; TopoI_cat_a/b-sub_euk.
DR   InterPro; IPR013500; TopoI_cat_euk.
DR   InterPro; IPR008336; TopoI_DNA-bd_euk.
DR   InterPro; IPR036202; TopoI_DNA-bd_euk_N_sf.
DR   InterPro; IPR013499; TopoI_euk.
DR   Pfam; PF14370; Topo_C_assoc; 1.
DR   Pfam; PF01028; Topoisom_I; 1.
DR   Pfam; PF02919; Topoisom_I_N; 1.
DR   PRINTS; PR00416; EUTPISMRASEI.
DR   SMART; SM00435; TOPEUc; 1.
DR   SUPFAM; SSF56349; SSF56349; 1.
DR   SUPFAM; SSF56741; SSF56741; 1.
DR   PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2Q8K2.
DR   SWISS-2DPAGE; A2Q8K2.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|RuleBase:RU365101};
KW   Isomerase {ECO:0000256|RuleBase:RU365101, ECO:0000313|EMBL:CAK36999.1};
KW   Topoisomerase {ECO:0000256|RuleBase:RU365101}.
FT   DOMAIN          406..856
FT                   /note="TOPEUc"
FT                   /evidence="ECO:0000259|SMART:SM00435"
FT   REGION          1..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          768..788
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          803..830
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..19
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..114
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..162
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..200
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..217
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   884 AA;  100805 MW;  AC6F6F7F48AA7FBD CRC64;
     MSSSEDDTPL VQANGRRISS HTDSKMRDAT ETNGHVDPGV SIRFGPVQAE NDVDMADADA
     AAVPKRKSRS SVGQRKSYAE PESSEEDDQP LSKRRRTSVK HEDPETDDDV PLALNGRKLP
     KASETAIGEE SDSDVPIERK LASQKKKIQQ KAEKDAKVTR KPAPPKTTKT AATKRQTNGV
     KKEPEDVKPS TVKKTAKPTK ASDKAALSSQ VKRAASSAKS TPVKKEESEE AEDADEEEYR
     WWEDPTKGDG TIKWTTLEHN GVVFPPPYEP LPKNVKMKYD GIPVTLHPDA EEVAGFFGGM
     LNATQHVENP TFQKNFFMDF RDILKKTGGA KDPKGNKVDI KDFHKCDFQP IFAYYDNQRQ
     EKKALPPAEK KRLKAEKDAQ EAPYMFCMWD GRKQKVGNFR VEPPALFRGR GEHPKTGRVK
     SRVQPEQITI NIGKDAPVPP PPEGHKWKEV KHDQEGTWLA MWQENINGNY KYVMLAANSD
     VKGQSDYKKF EKARELKHHI GRIRKDYQKN LKHELMVERQ KATAVYLIDQ FALRAGNEKG
     EDEAETVGCC SLKYENVTLK PPNKVVFDFL GKDSIRFYDE VEVDAQVFKN LKIFKKAPKK
     EGDEIFDRLT TSALNKHLSA YMQGLTAKVF RTYNASHTMS TLLKDMKATG NIAEKVKAYN
     DANRKVAILC NHKRTVAASH ANQMEKMSER IKGLRYQRWR LKQQMLDLEP SLKKKKGAKY
     FEMDEDMDLE WVKEHQAFLV EEQRQKIQKK FEKDNEKLAA EGEKEMKATE LESRLQVAKD
     LEKKFNKENK TGKVEAEGKA PTVDKIEAAI TKLEQRIETM ELQAQDKEEN KEVALGTSKI
     NYIDPRLTVV FSKKFDVPIE KFFSKSLREK FEWAIKSVDE DWEF
//

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