TOP1_CANAR
ID TOP1_CANAR Reviewed; 749 AA.
AC A0A0L0P4F8;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=DNA topoisomerase 1 {ECO:0000305};
DE EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10130};
DE AltName: Full=DNA topoisomerase I {ECO:0000305};
GN Name=TOP1; ORFNames=QG37_01781;
OS Candida auris (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis.
OX NCBI_TaxID=498019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6684;
RX PubMed=26346253; DOI=10.1186/s12864-015-1863-z;
RA Chatterjee S., Alampalli S.V., Nageshan R.K., Chettiar S.T., Joshi S.,
RA Tatu U.S.;
RT "Draft genome of a commonly misdiagnosed multidrug resistant pathogen
RT Candida auris.";
RL BMC Genomics 16:686-686(2015).
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:0000255|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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10130};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P11387}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P11387}.
CC -!- SIMILARITY: Belongs to the type IB topoisomerase family. {ECO:0000305}.
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DR EMBL; LGST01000016; KNE00911.1; -; Genomic_DNA.
DR RefSeq; XP_018170634.1; XM_018311275.1.
DR AlphaFoldDB; A0A0L0P4F8; -.
DR SMR; A0A0L0P4F8; -.
DR EnsemblFungi; KNE00911; KNE00911; QG37_01781.
DR VEuPathDB; FungiDB:B9J08_003421; -.
DR VEuPathDB; FungiDB:CJI96_0002046; -.
DR VEuPathDB; FungiDB:CJI97_003496; -.
DR VEuPathDB; FungiDB:CJJ07_001114; -.
DR VEuPathDB; FungiDB:CJJ09_000684; -.
DR VEuPathDB; FungiDB:QG37_01781; -.
DR Proteomes; UP000037122; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:EnsemblFungi.
DR GO; GO:0006265; P:DNA topological change; IEA:EnsemblFungi.
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 assembly; 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 from RNA polymerase II promoter; IEA:EnsemblFungi.
DR CDD; cd00659; Topo_IB_C; 1.
DR Gene3D; 1.10.10.41; -; 1.
DR Gene3D; 1.10.132.10; -; 1.
DR Gene3D; 2.170.11.10; -; 1.
DR Gene3D; 3.90.15.10; -; 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 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; SSF56349; 1.
DR SUPFAM; SSF56741; SSF56741; 1.
DR PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE 3: Inferred from homology;
KW DNA-binding; Isomerase; Nucleus; Topoisomerase.
FT CHAIN 1..749
FT /note="DNA topoisomerase 1"
FT /id="PRO_0000447628"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..339
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11387"
FT REGION 401..406
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11387"
FT REGION 493..495
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11387"
FT COMPBIAS 87..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 707
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10130"
FT SITE 277
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11387"
FT SITE 325
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11387"
FT SITE 356
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11387"
FT SITE 413
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11387"
FT SITE 439
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11387"
FT SITE 482
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11387"
FT SITE 539
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11387"
FT SITE 557
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11387"
SQ SEQUENCE 749 AA; 86838 MW; C5D65A3332875F72 CRC64;
MSDSEDVALS ELSSRNGIKK EDEEMPLAQL NGNGNAKLRK RKHSEKSKDD HKDKKRKKEK
KLSKEKVNNK VKDELISAPV TPKKTPKISK TPVSATSSPA PKKEDSVETD EGYKWWEDEN
FGEGDERWQT LEHNGVLFPP PYEPLPSYVK LYYEGKPVDL PPLAEEVAGY FAAMIETDHA
KNPVFQQNFF NDFLQVLKEG GGCNVDIKEF SKCDFSKMAA FFEKQREEKK SMSKAEKQRI
KEEKEKLEEP FKTCLMDGRR ENVGNFRVEP PGLFRGRGAH PKTGKFKRRV FPEDITLNLG
EGAPIPPPPE GHQWGGIRHD KTVVWLAMWR ENISDTFKYV KLAANSSIKG ISDMKKFETA
RKLKDHIERI RADYQKMLKD QFMQNRQIAT ATYLIDIFAL RAGGEKGEDE ADTVGCCSLR
YEHVTLKPPN KVIFDFLGKD SIRFYQEVEV DRQVFKNLRI FKKEPKGPGD DLFDRITPTI
LNKHLQNYMK GLTAKVFRTY NASKTMQDQM DLISNEGTVA EKVVKYNAAN RTVAILCNHQ
RTVSKNHEQA VKRINDKIRE LEWQKIRLKK MILDIDETEK KDNPKYFEEL DDLTNDEMNV
IVERVIERQK DQAEKKWNRD NEKRKMEKEE LLTKADLQEK LDKIEETRKD YLEEIKTGVV
RATKGSSVSS LKSKVETVEN RIVNTSYQLK DKEDNSEVSL GTSKMNYIDP RLTVVFAKKF
NVPIEKLFTK TLRDKFNWAI ESTDENWRF
