TOP3_CAEEL
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 03-AUG-2022, entry version 143.
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. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 STRING; 6239.Y56A3A.27; -.
DR EPD; O61660; -.
DR PaxDb; O61660; -.
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 CTD; 176631; -.
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; EHICFEV; -.
DR OrthoDB; 373433at2759; -.
DR PhylomeDB; O61660; -.
DR BRENDA; 5.6.2.1; 1045.
DR Reactome; R-CEL-5693607; Processing of DNA double-strand break ends.
DR PRO; PR:O61660; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006596; Expressed in gonad and 5 other 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; 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 InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR11390; PTHR11390; 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; SSF56712; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 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 ZN_FING 715..759
FT /note="GRF-type"
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:0000250"
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
