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Database: UniProt
Entry: L8X1W4_THACA
LinkDB: L8X1W4_THACA
Original site: L8X1W4_THACA 
ID   L8X1W4_THACA            Unreviewed;       925 AA.
AC   L8X1W4;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   03-MAY-2023, entry version 41.
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=AG1IA_03338 {ECO:0000313|EMBL:ELU42619.1};
OS   Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS   (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU42619.1, ECO:0000313|Proteomes:UP000011668};
RN   [1] {ECO:0000313|EMBL:ELU42619.1, ECO:0000313|Proteomes:UP000011668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX   PubMed=23361014; DOI=10.1038/ncomms2427;
RA   Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA   Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA   Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA   Wang L., Liu H., Li P.;
RT   "The evolution and pathogenic mechanisms of the rice sheath blight
RT   pathogen.";
RL   Nat. Commun. 4:1424-1424(2013).
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:ELU42619.1}.
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DR   EMBL; AFRT01000780; ELU42619.1; -; Genomic_DNA.
DR   AlphaFoldDB; L8X1W4; -.
DR   STRING; 983506.L8X1W4; -.
DR   HOGENOM; CLU_009193_1_0_1; -.
DR   Proteomes; UP000011668; 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   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:UP000011668};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW   ECO:0000256|RuleBase:RU365101}.
FT   DOMAIN          449..898
FT                   /note="DNA topoisomerase I eukaryotic-type"
FT                   /evidence="ECO:0000259|SMART:SM00435"
FT   REGION          1..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   925 AA;  104147 MW;  7EB39D24CF46A37E CRC64;
     MARRVTSDSE SGDDAPLAQS LTATSRATSK RPRPSASADG GPAKRPRSTV NSDDSGPDVA
     RPAKQLAAAA VPLPGALKKS NGKSRTPASK KDMTELGQHE AAVPLVKTED GDVDMADADE
     SDDEPLNKRI KAAANGKSKS KPVSSRMKTK APVKKESSDD SDDDDDDDDN SVTRNKNGAN
     ESGEEEVSAS ESESEPDVPL SKKKSAARKK VKQESDEDED VKPARKTPKK NGKAVKKEES
     DDDVKPSKGK AKVKKEDGDK KLSARALKKQ KEEEEEAERF KWYVVVLLLS SHPHPSPGGR
     LKLWAMVPPN GQPSSMLAYS SLLPTNLYPS KEVDLPPESE ELAGWFGALL ETEHAADEVF
     QKNFFGDWQA VLKDHPPRNG IVIKDFDKCD FRPMFDFFEA EKAKKKSMTA AEKKAIKEAK
     SKDEEKYTAC TMDGRPEKVG NFRIEPPGLF RGRGKHPKKG KHKYRLRPED ITINIGQNAP
     IPVPNIPGKW GKIQHDQTVT WLASWKENVN GNFKYVFLAA GSSLKGQSDM QKFEKARELK
     KHVDRIREDY TRDLKNKTSA DRQRATAMYF IDRLALRAGN EKGEDEADTV GCCSLRYEHI
     MLEPPNKLIF DFLGKDSIRY YNVVEVEPQI FKNIRIFKGD GKSEGDALFD RVSTGGLNKH
     LNSYMKGLSA KVFRTYNASI TFQKQLDENT PADADITQKL AAYNRANRMV AILCNHQKSV
     SKNHDASMGK LGDQLRGLKY NRMKLRHQLF TLDKKLKKKH PELDELESDL DDEFIERWED
     AKREEDIAKA RKKFEKDNEK RVEKGEKEEK ESALDEKIDD INAEYDRLKE ERGTEQAAGP
     KGRTPEKVLD AITKLDEKIK MFKFKMQDKE EGKEVALGTS KINYLDPRIT AAWCKKHDVP
     IEKIFAKTLL NKFPWAMEID EDWKF
//
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