TOP1_CANAX
ID TOP1_CANAX Reviewed; 778 AA.
AC Q00313; P78593;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=DNA topoisomerase 1;
DE EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10130};
DE AltName: Full=DNA topoisomerase I;
GN Name=TOP1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10231 / CBS 6431 / CIP 48.72 / DSM 1386 / NBRC 1594;
RX PubMed=9026437; DOI=10.1111/j.1574-6968.1996.tb08143.x;
RA Taylor A., Giles K., Sarthy A.V., McGonigal T., Fostel J.;
RT "Identification of the gene encoding DNA topoisomerase I from Candida
RT albicans.";
RL FEMS Microbiol. Lett. 138:113-121(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9043115; DOI=10.1099/00221287-143-2-377;
RA Jiang W., Gerhold D., Kmiec E.B., Hauser M., Becker J.M., Koltin Y.;
RT "The topoisomerase I gene from Candida albicans.";
RL Microbiology 143:377-386(1997).
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 a target site in duplex
CC DNA. The scissile phosphodiester is attacked by the catalytic tyrosine
CC of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-
CC enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free
CC DNA strand then rotates around the intact phosphodiester bond on the
CC opposing strand, thus removing DNA supercoils. Finally, in the
CC religation step, the DNA 5'-OH attacks the covalent intermediate to
CC expel the active-site tyrosine and restore the DNA phosphodiester
CC backbone (By similarity). {ECO:0000250}.
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 -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC negative and positive supercoils, whereas prokaryotic enzymes relax
CC only negative supercoils.
CC -!- SIMILARITY: Belongs to the type IB topoisomerase family. {ECO:0000305}.
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DR EMBL; U40454; AAC49381.1; -; Genomic_DNA.
DR EMBL; U41342; AAB39507.1; -; Genomic_DNA.
DR AlphaFoldDB; Q00313; -.
DR SMR; Q00313; -.
DR VEuPathDB; FungiDB:C6_00950C_A; -.
DR VEuPathDB; FungiDB:CAWG_05264; -.
DR PHI-base; PHI:80; -.
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-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; Topoisomerase.
FT CHAIN 1..778
FT /note="DNA topoisomerase 1"
FT /id="PRO_0000145208"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..368
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 430..435
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 522..524
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT COMPBIAS 33..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 736
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT SITE 306
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 354
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 385
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 442
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 468
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 511
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 568
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 586
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="N -> S (in Ref. 2; AAB39507)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="K -> KRK (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="L -> F (in Ref. 2; AAB39507)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="I -> L (in Ref. 2; AAB39507)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="R -> K (in Ref. 2; AAB39507)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 778 AA; 90484 MW; BFABE6B22EA2E5D3 CRC64;
MNSSDEEDIA LSRLAKKSSS ITSASTYEDD EDDDIPLAKK SRKKRVESDY EEDEDEVPLK
KLSNGRAKKQ VKTETKVKKE PKSANKSKST SKKDTKVKKE KTTVKKESKA TSTKVKEESK
TQSDSQASVK SETPEEDQGY KWWEVNQEEE GDGYIKWQTL EHNGVMFPPP YEPLPSHVKL
YYNNKPVNLP PEAEEVAGFY GAMLETDHAK NPVFQKNFFN DFLEVLKECG GCGVEIKKFE
KLDFSKMYAH FEKLREEKKA MSREEKKRIK EEKEKEEEPY RTCYLNGRKE LVGNFRIEPP
GLFRGRGAHP KTGKLKRRVV SEQVTLNLGK DAKIPEPPAG HQWGEIRHDN EVTWLAMWKE
NISDSLKYVR FANNSSVKGQ SDFKKFETAR KLRDHVDSIR KDYTKMLKSE KMQDRQMATA
MYLIDVFALR AGGEKGEDEA DTVGCCSLRY EHVTLKPPNK VIFDLLGKDS IRFYQEVEVD
KQVFKNLRIF KKSPKQPGDD LFDRINPSLV NRQLQNYMKG LTAKVFRTYN ASKTMQDQID
IIENEGTVAE KVAKFNAANR TVAILCNHQR TVSKTHGDSV QRINDKLKKF MWQKIRLKKM
ILQLEPKLKK KDSKYFEEID DLIKEDIEHI HHTIIKRQRE QAKKKLERDN EKLKLEGKPL
LTESDIKDKL DKIDELEKEY QKELKTGKPI VTKNATVEKL KQQIETLENR ILNVSIQLKD
KEDNSEVSLG TSKMNYIDPR LIVMFSKKFD VPIEKLFTKT LREKFIWAIE SADENWRF
