ID A0A1C1CLM2_9EURO Unreviewed; 916 AA.
AC A0A1C1CLM2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 Name=TOP1 {ECO:0000313|EMBL:OCT49406.1};
GN ORFNames=CLCR_04549 {ECO:0000313|EMBL:OCT49406.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT49406.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-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}.
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:OCT49406.1}.
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DR EMBL; LGRB01000011; OCT49406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1CLM2; -.
DR STRING; 86049.A0A1C1CLM2; -.
DR VEuPathDB; FungiDB:CLCR_04549; -.
DR VEuPathDB; FungiDB:G647_03320; -.
DR eggNOG; KOG0981; Eukaryota.
DR Proteomes; UP000094526; 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 CDD; cd00660; Topoisomer_IB_N; 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; 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: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.
DR PROSITE; PS00176; TOPOISOMERASE_I_EUK; 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:UP000094526};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU365101}.
FT DOMAIN 438..888
FT /note="DNA topoisomerase I eukaryotic-type"
FT /evidence="ECO:0000259|SMART:SM00435"
FT REGION 1..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 800..862
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 87..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 103833 MW; 43DB421C74F05ADF CRC64;
MSSSDDDIPL AGKRKSNGTN GVQIVAPHLS ADKIPSSVDA TLDRQIPSNG NVMPGISIAH
GEVKTEDASP SDAKGDLVNG AGAGKRKFRE SVTRPDYADA ESSDDDVPLS KKRRTSTAVE
SDSDDAPLMA KAKSNDKVVK MPPRLSAHQI GEDSDSDVPL GQKLAKQKQK IEKAAEKEAK
QIRKEEKQES AKAPKKAPPA KRVKKEESSD DEKPLSKRAP PKKAKAEPAG PSKKVKSEPG
STTKKPAAAP KAVKKEESAD PDDEEDEEED IKWWEDPTKG DGTNKWETLQ HSGVVFPPPY
KPLPKNVKMK YDGEPITLHP DAEEVAGFFG SMLNSTHNVE NPTFQKNFFH DFKEILKKTG
GAKNRNGEKV EIKEFAKCDF RPIFEHYEAE RAAKKALSRE EKKALKQEKD EAEAPYMYCI
WDGKKQKVGN FRVEPPGLFR GRGDHPKTGH VKTRVMPEQI TINIGKEATV PVPPEGHSWK
EIKHDKQGTW LAMWQENING NYKYVMLAAN SDIKGQSDYK KFEKARELKK HIDRIRKDYQ
KDLKAEPTVD RQRATAMYLI DRFALRAGNE KGDDEADTVG CCSLKYENVT LRPPNVVIFD
FLGKDSIRFH EEFEVDPQVF KNLKIFKRPP KHEGDALFDR LSTSALNKHL KSYMDGLTAK
VFRTYNASYT MSKLLSEMKS EGSLAERVKD YNDANRRVAI LCNHKRTVGA GHAGQMEKLG
DRIKGLKYQQ WRMKQMMIDV DPKIKKKKGA EYFELPDDID EAWILEHQAF LVEQEKTKIT
KKFEKDNEKR KADGEKEMKH KELEERLKAA TELEKKFKKE NKTKKVEAEG KSPSVEKFEE
QIKKLDTRIA TMAIQAEDKE NNKEVALGTS KINYIDPRLT VVFSKKFNVP IEKFFSKTLR
EKFEWALKSV DENWTF
//
