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Database: UniProt
Entry: A0A0C3LE35_9AGAM
LinkDB: A0A0C3LE35_9AGAM
Original site: A0A0C3LE35_9AGAM 
ID   A0A0C3LE35_9AGAM        Unreviewed;       458 AA.
AC   A0A0C3LE35;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   03-MAY-2023, entry version 32.
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};
DE   Flags: Fragment;
GN   ORFNames=M407DRAFT_66929 {ECO:0000313|EMBL:KIO32203.1};
OS   Tulasnella calospora MUT 4182.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Tulasnellaceae; Tulasnella.
OX   NCBI_TaxID=1051891 {ECO:0000313|EMBL:KIO32203.1, ECO:0000313|Proteomes:UP000054248};
RN   [1] {ECO:0000313|EMBL:KIO32203.1, ECO:0000313|Proteomes:UP000054248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUT 4182 {ECO:0000313|EMBL:KIO32203.1,
RC   ECO:0000313|Proteomes:UP000054248};
RG   DOE Joint Genome Institute;
RA   Kuo A., Girlanda M., Perotto S., Kohler A., Nagy L.G., Floudas D.,
RA   Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA   Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUT 4182 {ECO:0000313|Proteomes:UP000054248};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KN822956; KIO32203.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C3LE35; -.
DR   STRING; 1051891.A0A0C3LE35; -.
DR   HOGENOM; CLU_009193_2_0_1; -.
DR   OrthoDB; 10940at2759; -.
DR   Proteomes; UP000054248; 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   InterPro; IPR011010; DNA_brk_join_enz.
DR   InterPro; IPR013030; DNA_topo_DNA_db_N_dom2.
DR   InterPro; IPR001631; TopoI.
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.
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:UP000054248};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW   ECO:0000256|RuleBase:RU365101}.
FT   DOMAIN          1..418
FT                   /note="DNA topoisomerase I eukaryotic-type"
FT                   /evidence="ECO:0000259|SMART:SM00435"
FT   COILED          331..358
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KIO32203.1"
SQ   SEQUENCE   458 AA;  52714 MW;  E81DD31423AADC31 CRC64;
     IPTPNVPGKW GNIVHDNTVT WLATWKENIN GNFKYVFLAA GSSIKGQSDM AKFEKARELK
     KHVARIRQDY TAELRSKVTA ERQRATAMYF IDKLALRAGN EKGEDEADTV GCCSLRYEHV
     TLEPPNKLVF DFLGKDSIRY FNTVEVDPQV FKNMRIFKGN GKEEKDPIFD RVTTGGLNKH
     LQSYMKGLTA KVFRTYNASI TFQQQLDANT RKDMTDAEKL AAYHEANRMV AILCNHQKSV
     SKGHGASMEK MSDKLRGLKY QRMKLRKVLF TMDPKMKKKR PELTELESDL DDDFIEYWEE
     ELKKKDIEKA TKKFEKNNET RAEKGEKPEP QKKLDETIKK VEAEYKELKA ERKSKDVNIG
     SFKDPEKVLA NIEKIDERIQ TFKINMEVKD KGKDVALGTS KINYLDPRIT ASWCKTYNIP
     IEKLFSKTLI VKCRRSPVLS NASLCSLLFP LQSLGHSR
//
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