ID   TOP3_CAEEL              Reviewed;         759 AA.
AC   O61660; Q9U223;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 151.
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=top-3 {ECO:0000312|WormBase:Y56A3A.27};
GN   ORFNames=Y56A3A.27 {ECO:0000312|WormBase:Y56A3A.27};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Bristol N2;
RX   PubMed=10756204; DOI=10.1093/nar/28.9.2012;
RA   Kim Y.-C., Lee J., Koo H.-S.;
RT   "Functional characterization of Caenorhabditis elegans DNA topoisomerase
RT   IIIalpha.";
RL   Nucleic Acids Res. 28:2012-2017(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   INTERACTION WITH RMH-1.
RX   PubMed=27011106; DOI=10.1371/journal.pbio.1002412;
RA   Jagut M., Hamminger P., Woglar A., Millonigg S., Paulin L., Mikl M.,
RA   Dello Stritto M.R., Tang L., Habacher C., Tam A., Gallach M.,
RA   von Haeseler A., Villeneuve A.M., Jantsch V.;
RT   "Separable roles for a Caenorhabditis elegans RMI1 homolog in promoting and
RT   antagonizing meiotic crossovers ensure faithful chromosome inheritance.";
RL   PLoS Biol. 14:E1002412-E1002412(2016).
RN   [4]
RP   FUNCTION, IDENTIFICATION IN BTR COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=34252074; DOI=10.1371/journal.pgen.1009663;
RA   Velkova M., Silva N., Dello Stritto M.R., Schleiffer A., Barraud P.,
RA   Hartl M., Jantsch V.;
RT   "Caenorhabditis elegans RMI2 functional homolog-2 (RMIF-2) and RMI1 (RMH-1)
RT   have both overlapping and distinct meiotic functions within the BTR
RT   complex.";
RL   PLoS Genet. 17:e1009663-e1009663(2021).
CC   -!- FUNCTION: Component of the BTR double Holliday Junction dissolution
CC       complex, which is involved in homologous recombination during meiotic
CC       double strand break in the germline (Probable). Releases the
CC       supercoiling and torsional tension of DNA introduced during the DNA
CC       replication and transcription by transiently cleaving and rejoining one
CC       strand of the DNA duplex. Introduces a single-strand break via
CC       transesterification at a target site in duplex DNA. The scissile
CC       phosphodiester is attacked by the catalytic tyrosine of the enzyme,
CC       resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme
CC       intermediate and the expulsion of a 3'-OH DNA strand. The free DNA
CC       strand than undergoes passage around the unbroken strand thus removing
CC       DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks
CC       the covalent intermediate to expel the active-site tyrosine and restore
CC       the DNA phosphodiester backbone (By similarity). {ECO:0000250,
CC       ECO:0000305|PubMed:34252074}.
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: Component of the BTR double Holliday Junction dissolution
CC       complex composed of at least him-6, top-3, rmh-1 and rmif-2, which is
CC       involved in double strand break repair in the germline (Probable). May
CC       interact with rmh-1 (PubMed:27011106). {ECO:0000269|PubMed:27011106,
CC       ECO:0000305|PubMed:34252074}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:34252074}.
CC       Note=Localizes to nuclear foci throughout pachynema in meiotic prophase
CC       I during meiotic recombination (PubMed:34252074). Localization at
CC       nuclear foci is dependent on rmif-2 (PubMed:34252074).
CC       {ECO:0000269|PubMed:34252074}.
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01383, ECO:0000305}.
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DR   EMBL; AF057032; AAC13567.1; -; mRNA.
DR   EMBL; BX284603; CAB60518.2; -; Genomic_DNA.
DR   PIR; T43031; T43031.
DR   RefSeq; NP_499558.1; NM_067157.4.
DR   AlphaFoldDB; O61660; -.
DR   SMR; O61660; -.
DR   BioGRID; 41811; 7.
DR   ComplexPortal; CPX-7361; BTR double Holliday Junction dissolution complex.
DR   STRING; 6239.Y56A3A.27.1; -.
DR   EPD; O61660; -.
DR   PaxDb; 6239-Y56A3A-27; -.
DR   PeptideAtlas; O61660; -.
DR   EnsemblMetazoa; Y56A3A.27.1; Y56A3A.27.1; WBGene00006596.
DR   GeneID; 176631; -.
DR   KEGG; cel:CELE_Y56A3A.27; -.
DR   UCSC; Y56A3A.27.1; c. elegans.
DR   AGR; WB:WBGene00006596; -.
DR   WormBase; Y56A3A.27; CE28138; WBGene00006596; top-3.
DR   eggNOG; KOG1956; Eukaryota.
DR   GeneTree; ENSGT00940000156701; -.
DR   HOGENOM; CLU_002929_1_2_1; -.
DR   InParanoid; O61660; -.
DR   OMA; VEHCRYR; -.
DR   OrthoDB; 166270at2759; -.
DR   PhylomeDB; O61660; -.
DR   BRENDA; 5.6.2.1; 1045.
DR   PRO; PR:O61660; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00006596; Expressed in gonad and 5 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003916; F:DNA topoisomerase activity; IBA:GO_Central.
DR   GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IDA:WormBase.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IDA:WormBase.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR   Gene3D; 3.40.50.140; -; 1.
DR   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR   Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR   Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 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   InterPro; IPR010666; Znf_GRF.
DR   PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF06839; zf-GRF; 1.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   PROSITE; PS00396; TOPO_IA_1; 1.
DR   PROSITE; PS52039; TOPO_IA_2; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
DR   PROSITE; PS51999; ZF_GRF; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Isomerase; Metal-binding; Nucleus; Reference proteome;
KW   Topoisomerase; Zinc; Zinc-finger.
FT   CHAIN           1..759
FT                   /note="DNA topoisomerase 3"
FT                   /id="PRO_0000145194"
FT   DOMAIN          3..147
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT   DOMAIN          165..590
FT                   /note="Topo IA-type catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
FT   ZN_FING         716..759
FT                   /note="GRF-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01343"
FT   REGION          609..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        334
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
FT   BINDING         716
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01343"
FT   BINDING         718
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01343"
FT   BINDING         743
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01343"
FT   BINDING         753
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01343"
SQ   SEQUENCE   759 AA;  85438 MW;  3D862412D72946BD CRC64;
     MKRALFVAEK NDVAKGVAAI LSNGTANRRE GRSKFNKIYT LNTELFGQQT AISVTSVSGH
     MMNFQFHENM SNWQTASMVE LFRAPVRHVV TPEMKLIEQT LREQAQRHDI LVVWTDCDRE
     GEAIGAEIVK VCRDSNRRLD IFRARFSEIT KAAITRAARN LIRLDEKTVA AVDCRSELDL
     RIGSAFTRLQ TLHLRNRFRD LLGQNDTSQV ISYGSCQFPT LGFVTDRYKM IENFVSEPFW
     KLIVEHTRES HKVEFLWDRN RLFDRDTVDI LHDECKETKE AHVEKVAKKP KSKWRPQALD
     TVELEKLGIS KLRMSAKQTM QVAEKLYSKG FISYPRTETN KFPAGLNLTP LVQQQTQSNI
     WGDFANEVLQ NGVNPRNGRK SDEAHPPIHP LKFTEKHQLQ GDDWKVYELV VRHFLACVSQ
     DAQGEETMVN LTVGTEKFHA SGLRIRDMGY LKVYVYEKWG NRLLPTYTEG ERFTDFELKI
     GDGKTQAPDF LTEADLISLM DKYGIGTDAT HAEHIEKIKT REYIGVRPDG KLIPSFLGLA
     LVDGYDDMGF AMSKPDLRAN LEIGLKEICD GRRQKQEVLD EQIGKYRAIF VESERKIGVL
     SQSLQRYLDK NNQAGGGPGG PGGGGGPPRG PGGGGGGGPT GPPAPPKPPA KPRGRPPRKS
     ISPAVKNGHD DPENDTIVTL SEVFGSMSNP KPARKPRAPR KSAAPKEQEE EEEVFCQCPE
     PMRAVTKVVQ KEGPNKGKKF YTCSLPYTSS EKCNFFKWA
//