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Database: UniProt
Entry: A0A1B7TC55_9ASCO
LinkDB: A0A1B7TC55_9ASCO
Original site: A0A1B7TC55_9ASCO 
ID   A0A1B7TC55_9ASCO        Unreviewed;       773 AA.
AC   A0A1B7TC55;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   03-MAY-2023, entry version 31.
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=HANVADRAFT_53270 {ECO:0000313|EMBL:OBA26297.1};
OS   Hanseniaspora valbyensis NRRL Y-1626.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX   NCBI_TaxID=766949 {ECO:0000313|EMBL:OBA26297.1, ECO:0000313|Proteomes:UP000092321};
RN   [1] {ECO:0000313|Proteomes:UP000092321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-1626 {ECO:0000313|Proteomes:UP000092321};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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|ARBA:ARBA00000213,
CC         ECO:0000256|RuleBase:RU365101};
CC   -!- SIMILARITY: Belongs to the type IB topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00006645, ECO:0000256|RuleBase:RU365101}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBA26297.1}.
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DR   EMBL; LXPE01000020; OBA26297.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B7TC55; -.
DR   OrthoDB; 10940at2759; -.
DR   Proteomes; UP000092321; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
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; 1.10.132.10; -; 1.
DR   Gene3D; 2.170.11.10; DNA Topoisomerase I, domain 2; 1.
DR   Gene3D; 1.10.10.41; Yeast DNA topoisomerase - domain 1; 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   PANTHER; PTHR10290:SF3; DNA TOPOISOMERASE 1; 1.
DR   PANTHER; PTHR10290; DNA TOPOISOMERASE I; 1.
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; DNA breaking-rejoining enzymes; 1.
DR   SUPFAM; SSF56741; Eukaryotic DNA topoisomerase I, N-terminal DNA-binding fragment; 1.
DR   PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU365101};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU365101};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092321};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW   ECO:0000256|RuleBase:RU365101}.
FT   DOMAIN          291..745
FT                   /note="DNA topoisomerase I eukaryotic-type"
FT                   /evidence="ECO:0000259|SMART:SM00435"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          240..268
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          692..719
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        35..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   773 AA;  90196 MW;  B426D3EBDF3718D2 CRC64;
     MAVAKVRPRK QSSEKKATTK RTRKQSSSSS NNNDDDDEPL NKKLKSNGKN STNKNDEVKD
     EDIPLGQLEK TKSKTKVISP KEEDIENDNE LTLSQIKSNI DKSIQIEKVS NSSDNKSLTE
     NEEDSSEYKW WEEDLDDGTE KWQTLEHNGV LFPPAYESLP DLVRLIYDNK PVKLPAQAEE
     VAGFFGAMIN TDHAMNPVFQ ANFFKDFLAV LKEAGGVLEP KNLKITKFDK CNFQPIFDYY
     EQKKEEKRQL SRTEKKALKE EKELLEESYK FCYLNGRKEQ VGNFRVEPPS LFRGRGKHPK
     TGSLKRRVYP EDIILNLGKN ATVPNPPAGH QWGEIRHDNT VQWLAMWKEN IFNSFKYVRF
     AANSSLKGIS DYKKFEKARE LKNHIEKIRQ DYREKLHSKV TFERQIAVAT YLIDVFALRA
     GGEKGEDEAD TVGCCSLRYE HITLTPPNNV TFDFLGKDSI RFYQEVVVDK QVFKSLKLFK
     KAPKKSGDQL FDRLDPSILN KHLQNYMPGL TAKVFRTYNA SKTMQDQLDG MEIKLEQPVQ
     EKILLYNAAN REVAILCNHQ RSVGKNHETS VQKATDKIEQ IIWQKIRFKR ALLQLNPKLK
     KTEGKMFEDI EDLTKEKELE IIKRVTERDL EKFKRKFLND NEKRKEKNEE LLPESQLEEW
     LDKVNKQKDL YIEELENDGK LSDEFMEKVS KEDKLRDKIH KFEQRIINAN LQLKDKEDNS
     QVSLGTSKIN YIDPRLSVVF CKRYNVPIEK VFTKTLRDKF KWAIEGVDDN WRF
//
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