ID W2RKA1_9EURO Unreviewed; 886 AA.
AC W2RKA1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=HMPREF1541_07884 {ECO:0000313|EMBL:ETN36897.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN36897.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN36897.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN36897.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) 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; KB822724; ETN36897.1; -; Genomic_DNA.
DR RefSeq; XP_008720429.1; XM_008722207.1.
DR AlphaFoldDB; W2RKA1; -.
DR STRING; 1220924.W2RKA1; -.
DR GeneID; 19975223; -.
DR VEuPathDB; FungiDB:HMPREF1541_07884; -.
DR eggNOG; KOG0981; Eukaryota.
DR HOGENOM; CLU_009193_1_1_1; -.
DR InParanoid; W2RKA1; -.
DR OrthoDB; 10940at2759; -.
DR Proteomes; UP000030752; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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; -; 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; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000030752};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU365101}.
FT DOMAIN 408..858
FT /note="DNA topoisomerase I eukaryotic-type"
FT /evidence="ECO:0000259|SMART:SM00435"
FT REGION 1..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 763..832
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 16..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 100881 MW; 492DA06BAE5076EC CRC64;
MASSSDDDMP ISKARKNGVN GTSAPPVSSA KIPSSLDRQM DKTLPTNGEI QPGISIRNGP
LTEDVEMKDT NGSAAPAKRK VSRPSYAEEE SSDDDKPIIK KRKTQPETAV ESDSDVPLAK
SKPNGKVAKK PPRASNQQIG EDSDSDVPIQ KKLIHEKQKI EAKAEKDAQK IRKADKPKKV
KKEESSDDDK PLKKTKPAPA AKAKTKVKVE SPAPKKAAGK KAAVKKEETE DPEEDDEDEG
TNWWDDPTKG DGTNKWETLQ HSGVVFPPPY QPLPKNVKLK YDGIPLTLHP DAEEVAGFFG
GMLNSTHNVE NPTFQKNFFN DFKEILKKTG GAKGPNGEKV DVKDFKKCDF KPIFDHYDAE
RAAKKALPAA EKKKLKAEKD AAEAPYMYCT WDGKKQKVGN FRVEPPGLFR GRGEHPKTGH
VKTRVPPEQI TLNIGKEATV PAPPEGHKWK EIKHDKQGTW LAMWQENING NYKYVMLAAN
SDVKGQSDYK KFEKARELKK HIDKIRKDYR KNLKAEMMAD RQKATAMYFI DQFALRAGNE
KGDDEAETVG CCSLKYEHIT LKEPNKVIFD FLGKDSIRFH EEFDVDQQVF KNLKIFKKAP
KGEGDDIFDR LTTTQLNNHL KNYMPGLTAK VFRTYNASYT MATLLKDMKA EGTHAEKVKA
YNDANRKVAI LCNHKRTVAA SHENTMEKLS ERIKAVKYQQ WRLKHMILDL DPKQKKKKGA
EWFELPDDMD EEWVKEHQAF LVEEAKNKIT KKFEKDNEKL KAEGEKEMKH KELEERLEAA
KELEKKYKKE NKTKKVEAEG KSITVEKLEE NIKKFDQRIE NMTVQAEDKE SNKEVALGTS
KINYIDPRLT VVFTKKFNVP IEKFFSKTLR EKFEWAIKSV EEDWEF
//
