TOP3_YEAST
ID TOP3_YEAST Reviewed; 656 AA.
AC P13099; D6VYN4;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=DNA topoisomerase 3;
DE EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10131};
DE AltName: Full=DNA topoisomerase III;
GN Name=TOP3; Synonyms=EDR1; OrderedLocusNames=YLR234W; ORFNames=L8083.3;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2546682; DOI=10.1016/0092-8674(89)90855-6;
RA Wallis J.W., Chrebet G., Brodsky G., Rolfe M., Rothstein R.;
RT "A hyper-recombination mutation in S. cerevisiae identifies a novel
RT eukaryotic topoisomerase.";
RL Cell 58:409-419(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 578-592; 605-615; 794-805 AND 1038-1046.
RX PubMed=8336724; DOI=10.1128/mcb.13.8.4884-4893.1993;
RA Jiang W., Middleton K., Yoon H.-J., Fouquet C., Carbon J.;
RT "An essential yeast protein, CBF5p, binds in vitro to centromeres and
RT microtubules.";
RL Mol. Cell. Biol. 13:4884-4893(1993).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP SUBUNIT.
RX PubMed=15889139; DOI=10.1038/sj.emboj.7600684;
RA Chang M., Bellaoui M., Zhang C., Desai R., Morozov P., Delgado-Cruzata L.,
RA Rothstein R., Freyer G.A., Boone C., Brown G.W.;
RT "RMI1/NCE4, a suppressor of genome instability, encodes a member of the
RT RecQ helicase/Topo III complex.";
RL EMBO J. 24:2024-2033(2005).
RN [7]
RP SUBUNIT.
RX PubMed=15899853; DOI=10.1128/mcb.25.11.4476-4487.2005;
RA Mullen J.R., Nallaseth F.S., Lan Y.Q., Slagle C.E., Brill S.J.;
RT "Yeast Rmi1/Nce4 controls genome stability as a subunit of the Sgs1-Top3
RT complex.";
RL Mol. Cell. Biol. 25:4476-4487(2005).
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-(5'-phosphotyrosyl)-
CC enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free
CC DNA strand than undergoes passage around the unbroken strand thus
CC removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH
CC attacks the covalent intermediate to expel the active-site tyrosine and
CC restore the DNA phosphodiester backbone (By similarity). Essential for
CC proper chromosome segregation in both meiosis and mitosis. Weakly
CC relaxes negative supercoils and displays a distinct preference for
CC binding single-stranded DNA. The TOP3-SGS1 protein complex may function
CC as a eukaryotic reverse gyrase introducing positive supercoils into
CC extrachromosomal ribosomal DNA rings. {ECO:0000250,
CC ECO:0000269|PubMed:2546682}.
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:PRU10131};
CC -!- SUBUNIT: Forms a complex with SGS1 and RMI1. Interacts with SGS1.
CC {ECO:0000269|PubMed:15889139, ECO:0000269|PubMed:15899853}.
CC -!- INTERACTION:
CC P13099; Q02685: RMI1; NbExp=9; IntAct=EBI-19365, EBI-38690;
CC P13099; P35187: SGS1; NbExp=6; IntAct=EBI-19365, EBI-17059;
CC -!- MISCELLANEOUS: Present with 468 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. {ECO:0000305}.
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DR EMBL; M24939; AAA35161.1; -; Genomic_DNA.
DR EMBL; U19027; AAB67406.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09550.1; -; Genomic_DNA.
DR PIR; A33169; ISBYT3.
DR RefSeq; NP_013335.1; NM_001182121.1.
DR AlphaFoldDB; P13099; -.
DR SMR; P13099; -.
DR BioGRID; 31503; 233.
DR ComplexPortal; CPX-1071; RecQ helicase-Topo III complex.
DR DIP; DIP-2912N; -.
DR IntAct; P13099; 5.
DR MINT; P13099; -.
DR STRING; 4932.YLR234W; -.
DR MaxQB; P13099; -.
DR PaxDb; P13099; -.
DR PRIDE; P13099; -.
DR EnsemblFungi; YLR234W_mRNA; YLR234W; YLR234W.
DR GeneID; 850935; -.
DR KEGG; sce:YLR234W; -.
DR SGD; S000004224; TOP3.
DR VEuPathDB; FungiDB:YLR234W; -.
DR eggNOG; KOG1956; Eukaryota.
DR GeneTree; ENSGT00940000156701; -.
DR HOGENOM; CLU_002929_1_1_1; -.
DR InParanoid; P13099; -.
DR OMA; TYPRVDT; -.
DR BioCyc; YEAST:G3O-32345-MON; -.
DR PRO; PR:P13099; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P13099; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031422; C:RecQ family helicase-topoisomerase III complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003916; F:DNA topoisomerase activity; IDA:SGD.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IDA:SGD.
DR GO; GO:0006265; P:DNA topological change; IDA:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0000018; P:regulation of DNA recombination; IMP:SGD.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IMP:SGD.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 1.10.290.10; -; 1.
DR Gene3D; 1.10.460.10; -; 1.
DR Gene3D; 2.70.20.10; -; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR023406; Topo_IA_AS.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013825; Topo_IA_cen_sub2.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR PANTHER; PTHR11390; PTHR11390; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; SSF56712; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Isomerase; Reference proteome;
KW Topoisomerase.
FT CHAIN 1..656
FT /note="DNA topoisomerase 3"
FT /id="PRO_0000145198"
FT DOMAIN 2..156
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT ACT_SITE 356
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 656 AA; 74371 MW; 51DF78936A88B4F4 CRC64;
MKVLCVAEKN SIAKAVSQIL GGGRSTSRDS GYMYVKNYDF MFSGFPFARN GANCEVTMTS
VAGHLTGIDF SHDSHGWGKC AIQELFDAPL NEIMNNNQKK IASNIKREAR NADYLMIWTD
CDREGEYIGW EIWQEAKRGN RLIQNDQVYR AVFSHLERQH ILNAARNPSR LDMKSVHAVG
TRIEIDLRAG VTFTRLLTET LRNKLRNQAT MTKDGAKHRG GNKNDSQVVS YGTCQFPTLG
FVVDRFERIR NFVPEEFWYI QLVVENKDNG GTTTFQWDRG HLFDRLSVLT FYETCIETAG
NVAQVVDLKS KPTTKYRPLP LTTVELQKNC ARYLRLNAKQ SLDAAEKLYQ KGFISYPRTE
TDTFPHAMDL KSLVEKQAQL DQLAAGGRTA WASYAASLLQ PENTSNNNKF KFPRSGSHDD
KAHPPIHPIV SLGPEANVSP VERRVYEYVA RHFLACCSED AKGQSMTLVL DWAVERFSAS
GLVVLERNFL DVYPWARWET TKQLPRLEMN ALVDIAKAEM KAGTTAPPKP MTESELILLM
DTNGIGTDAT IAEHIDKIQV RNYVRSEKVG KETYLQPTTL GVSLVHGFEA IGLEDSFAKP
FQRREMEQDL KKICEGHASK TDVVKDIVEK YRKYWHKTNA CKNTLLQVYD RVKASM
