ID H1UW96_COLHI Unreviewed; 918 AA.
AC H1UW96;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=CH063_04669 {ECO:0000313|EMBL:CCF32247.1}, CH63R_00491
GN {ECO:0000313|EMBL:OBR15311.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF32247.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|EMBL:CCF32247.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|EMBL:CCF32247.1};
RA Ma L.-J., O'Connell R., van Themaat E.V.L., Stueber K., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Colletotrichum higginsianum IMI 34906.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
RN [3] {ECO:0000313|EMBL:OBR15311.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|EMBL:OBR15311.1};
RA O'Connell R., Zambounis A., Thon M., Dallery J.-F.;
RT "Resequencing and annotation of the Colletotrichum higginsianum genome.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000092177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000092177};
RX PubMed=28851275; DOI=10.1186/s12864-017-4083-x;
RA Dallery J.-F., Lapalu N., Zampounis A., Pigne S., Luyten I., Amselem J.,
RA Wittenberg A.H.J., Zhou S., de Queiroz M.V., Robin G.P., Auger A.,
RA Hainaut M., Henrissat B., Kim K.-T., Lee Y.-H., Lespinet O., Schwartz D.C.,
RA Thon M.R., O'Connell R.J.;
RT "Gapless genome assembly of Colletotrichum higginsianum reveals chromosome
RT structure and association of transposable elements with secondary
RT metabolite gene clusters.";
RL BMC Genomics 18:667-667(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}.
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DR EMBL; CACQ02000367; CCF32247.1; -; Genomic_DNA.
DR EMBL; LTAN01000001; OBR15311.1; -; Genomic_DNA.
DR RefSeq; XP_018163828.1; XM_018295466.1.
DR STRING; 759273.H1UW96; -.
DR EnsemblFungi; CCF32247; CCF32247; CH063_04669.
DR GeneID; 28859573; -.
DR KEGG; chig:CH63R_00491; -.
DR VEuPathDB; FungiDB:CH63R_00491; -.
DR eggNOG; KOG0981; Eukaryota.
DR HOGENOM; CLU_009193_1_1_1; -.
DR OrthoDB; 10940at2759; -.
DR Proteomes; UP000007174; Unassembled WGS sequence.
DR Proteomes; UP000092177; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
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:0006271; P:DNA strand elongation involved in DNA replication; IEA:EnsemblFungi.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0007076; P:mitotic chromosome condensation; IEA:EnsemblFungi.
DR GO; GO:0007097; P:nuclear migration; IEA:EnsemblFungi.
DR GO; GO:0000183; P:rDNA heterochromatin formation; IEA:EnsemblFungi.
DR GO; GO:0000019; P:regulation of mitotic recombination; IEA:EnsemblFungi.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0009303; P:rRNA transcription; IEA:EnsemblFungi.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:EnsemblFungi.
DR CDD; cd00659; Topo_IB_C; 1.
DR CDD; cd03488; Topoisomer_IB_N_htopoI_like; 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; 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:SF23; 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 Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU365101}.
FT DOMAIN 436..889
FT /note="DNA topoisomerase I eukaryotic-type"
FT /evidence="ECO:0000259|SMART:SM00435"
FT REGION 1..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 801..856
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 50..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 104188 MW; 7D10BE0F2D6BD44F CRC64;
MSSSDDDAPL ARSNGHISAS RVSKADDFDM DRTASKARAA PPGLSIRHGP VDDEFMDIDG
PSTNGKRKSR SSLPKVNYKV DTESDDDAPL AKRQKTKPKI PETDSDDEPL TSKRGKNLPP
SYKETALPDE SSDDDQPLGA KLAKKKADIE KAAAKEARTI RASEAKAKKA TPKKAVKEES
SDDEPLAKSA TKKRQSNGAG SAKRKSNGMK VESDSDEPIA KKVAKKGTPA KAPAAKGKAA
ASAKAPGKKA DSKAKQESEA PEEEEEEEYE WWKDPKKEDD SVKWTTLEHN GVMFPPEYQP
LPKNVKLLYD GKPVNLPIEA EEVAGFFGAM LNSKHNVDNP VFQKNFFDDF KAVLKESGHA
TDKQGNKVDL KEFSKMNFEQ IFQYYEQQSA IRKTRSPAEK KAAKAEKDEL EAPFMYCKWD
GRKEKVGNFR VEPPSLFRGR GEHPKTGRLK KRVYPEQITI NIGKGAKIPE PPKGHKWKTV
VHDNKATWLA MWQENINGAY KYVMLGAASA IKGQSDMKKF EKARELKKHI DKIRRDYTKD
LKSEVMADRQ RATAVYLIDK FALRAGNEKD AENEAETVGC CSLKYEHITL REPNTVIFDF
LGKDSIRFYD EVTVEKQVFK NLKLFKKPPK TDGDDIFDRL TTTQLNNHLK NYMPGLTAKV
FRTYNASFTM STLLQKLVDH KNLTIAEKVK LYNDCNREVA ILCNHKRTVG AAHEAQMEKL
GDRIKGLRYQ QWRTKMMMLQ VDNKIKKKKG ADFFVRPEDL TDEWVLEHQQ FLVEEQRGKI
TKKFEKDNEK RLAEGQKPFP DKELKERLKA ADELAAKFKK ENKSKKVEPE GRSPSVEKLD
EQVKKFDDRV KTLELQAADR DGNKEVALST SKINYIDPRL TVVFAKKFDV PIEKFFSKTL
RDKFSWAIKS VEDEDWEF
//
