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Database: UniProt
Entry: A0A364L052_9EURO
LinkDB: A0A364L052_9EURO
Original site: A0A364L052_9EURO 
ID   A0A364L052_9EURO        Unreviewed;       852 AA.
AC   A0A364L052;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   08-NOV-2023, entry version 19.
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=BHQ10_005192 {ECO:0000313|EMBL:RAO69180.1};
OS   Talaromyces amestolkiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO69180.1, ECO:0000313|Proteomes:UP000249363};
RN   [1] {ECO:0000313|EMBL:RAO69180.1, ECO:0000313|Proteomes:UP000249363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIB {ECO:0000313|EMBL:RAO69180.1,
RC   ECO:0000313|Proteomes:UP000249363};
RX   PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA   de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA   Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT   "Differential ?-glucosidase expression as a function of carbon source
RT   availability in Talaromyces amestolkiae: a genomic and proteomic
RT   approach.";
RL   Biotechnol. Biofuels 10:161-161(2017).
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:RAO69180.1}.
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DR   EMBL; MIKG01000009; RAO69180.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A364L052; -.
DR   STRING; 1196081.A0A364L052; -.
DR   OrthoDB; 10940at2759; -.
DR   Proteomes; UP000249363; 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   CDD; cd03488; Topoisomer_IB_N_htopoI_like; 1.
DR   Gene3D; 1.10.132.10; -; 2.
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   InterPro; IPR048045; Topoisomer_I_DNA-bd.
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:UP000249363};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW   ECO:0000256|RuleBase:RU365101}.
FT   DOMAIN          374..824
FT                   /note="DNA topoisomerase I eukaryotic-type"
FT                   /evidence="ECO:0000259|SMART:SM00435"
FT   REGION          1..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          764..798
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        29..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   852 AA;  97004 MW;  4F006FB0931EC39A CRC64;
     MSSSDDDAPL LKASRTGALN PGVSIRFGPV DDEDVEMKDT KGVNGHKRRA RIGSGKQFYA
     EAESSEDEKP LSKKRRVSVK KQIDSDSEED IPLARKANGA RLPKASETAI GEESDSDIPI
     ERKLSKQKAN IEKKAEQEAK AIRKAEATSS TKKAKPKANG VKSENGVGAK KVIKSEPSTP
     AKKGKGKATP VKAESEDVEG ADEEEEYRWW EDPAKGDGTI KWTTLEHNGV VFPPDYEPLP
     KNVKMKYDGI PVVLHPEAEE VAGFFGSMLN STHNVENPTF QKNFFEDFKA ILKKTGGAKA
     QNGEPINIKE FKKCDFKPIF EYYDAKRLEK KAMSAAEKKA LKAEKDAAEA PYMYCMWDGR
     KQKVGNFRVE PPSLFRGRGE HPKTGRVKTR VMPEQITINI GKDAKVPPPP EGHKWKEVRH
     DQEGTWLAMW QENVNGNYKY VMLAANSDVK GQSDYKKFEK ARELKKHIDK IRADYQKGLK
     SELMADRQRA TAVYLIDKFA LRAGNEKGED EADTVGCCSL KYENISLRPP NTVIFDFLGK
     DSIRFYDEVE VDPQVFKNLK IFKKAPKKEG DEIFDRLTTS ALNKHLSNYM TGLTAKVFRT
     YNASYTFATL LKDMKAEGTV AEKVKQYNDA NRRVAILCNH KRTVTAGHAN QMEKLGDRIK
     GLRYQKWRVK MMMLDIDPTQ KKKKGAKYFE LDDDLDQAWI QEHQAFLVEE QRQKITKKFE
     KENEKLAADG EKEMKPRELE ERLVVVKDME KKFQKENKTG KVEVEGKGQT VEKLENNVTK
     LEQRIENMSL QAEDKENNKE VALGTSKINY IDPRLTVVFT KKFNVPIEKF FSKTLREKFD
     WAIKSVDENW EF
//
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