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
//