ID   TOP1_CANAL              Reviewed;         778 AA.
AC   Q00313; P78593;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 43.
DE   RecName: Full=DNA topoisomerase 1;
DE            EC=5.99.1.2;
DE   AltName: Full=DNA topoisomerase I;
GN   Name=TOP1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10321 / CCM 8215;
RX   MEDLINE=96242310; PubMed=9026437; DOI=10.1016/0378-1097(96)00059-6;
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   MEDLINE=97195784; PubMed=9043115;
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: The reaction catalyzed by topoisomerases leads to the
CC       conversion of one topological isomer of DNA to another.
CC   -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded
CC       DNA, followed by passage and rejoining.
CC   -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC       negative and positive supercoils, whereas prokaryotic enzymes
CC       relax only negative supercoils.
CC   -!- MISCELLANEOUS: When a topoisomerase transiently breaks a DNA
CC       backbone bond, it simultaneously forms a protein-DNA link, in
CC       which a tyrosyl oxygen in the enzyme is joined to a DNA phosphorus
CC       at one end of the enzyme-severed DNA strand.
CC   -!- SIMILARITY: Belongs to the eukaryotic type I topoisomerase family.
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DR   EMBL; U40454; AAC49381.1; -; Genomic_DNA.
DR   EMBL; U41342; AAB39507.1; -; Genomic_DNA.
DR   HSSP; P04786; 1OIS.
DR   BRENDA; 5.99.1.2; 1124.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0006268; P:DNA unwinding during replication; IEA:InterPro.
DR   InterPro; IPR018521; TopoI_AS.
DR   InterPro; IPR001631; TopoI_C.
DR   InterPro; IPR013499; TopoI_C_euk.
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; IPR013030; TopoI_DNA-bd_mixed-a/b_euk.
DR   InterPro; IPR008336; TopoI_DNA_bd_euk.
DR   Gene3D; G3DSA:3.90.15.10; TopoI_cat_a-hlx-sub_euk; 1.
DR   Gene3D; G3DSA:1.10.132.10; TopoI_cat_a/b-sub_euk; 1.
DR   Gene3D; G3DSA:2.170.11.10; TopoI_DNA-bd_mixed-a/b_euk; 1.
DR   Pfam; PF01028; Topoisom_I; 1.
DR   Pfam; PF02919; Topoisom_I_N; 1.
DR   PRINTS; PR00416; EUTPISMRASEI.
DR   SMART; SM00435; TOPEUc; 1.
DR   PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Isomerase; Nucleotide-binding;
KW   Topoisomerase.
FT   CHAIN         1    778       DNA topoisomerase 1.
FT                                /FTId=PRO_0000145208.
FT   ACT_SITE    736    736       O-(3'-phospho-DNA)-tyrosine intermediate.
FT   CONFLICT      2      2       N -> S (in Ref. 2; AAB39507).
FT   CONFLICT     61     61       K -> KRK (in Ref. 2).
FT   CONFLICT    465    465       L -> F (in Ref. 2; AAB39507).
FT   CONFLICT    623    623       I -> L (in Ref. 2; AAB39507).
FT   CONFLICT    710    710       R -> K (in Ref. 2; AAB39507).
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
//