TOP3_CANAR
ID TOP3_CANAR Reviewed; 640 AA.
AC A0A0L0P6P7;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=DNA topoisomerase 3 {ECO:0000305};
DE EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10131};
DE AltName: Full=DNA topoisomerase III {ECO:0000305};
GN Name=TOP3; ORFNames=QG37_00967;
OS Candida auris (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis.
OX NCBI_TaxID=498019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6684;
RX PubMed=26346253; DOI=10.1186/s12864-015-1863-z;
RA Chatterjee S., Alampalli S.V., Nageshan R.K., Chettiar S.T., Joshi S.,
RA Tatu U.S.;
RT "Draft genome of a commonly misdiagnosed multidrug resistant pathogen
RT Candida auris.";
RL BMC Genomics 16:686-686(2015).
CC -!- FUNCTION: Introduces a single-strand break via transesterification at a
CC target site in duplex DNA. Releases the supercoiling and torsional
CC tension of DNA introduced during the DNA replication and transcription
CC by transiently cleaving and rejoining one strand of the DNA duplex. The
CC scissile phosphodiester is attacked by the catalytic tyrosine of the
CC enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme
CC intermediate and the expulsion of a 3'-OH DNA strand.
CC {ECO:0000255|RuleBase:RU362092}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00995};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. {ECO:0000305}.
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DR EMBL; LGST01000007; KNE02028.1; -; Genomic_DNA.
DR RefSeq; XP_018171751.1; XM_018310517.1.
DR AlphaFoldDB; A0A0L0P6P7; -.
DR SMR; A0A0L0P6P7; -.
DR EnsemblFungi; KNE02028; KNE02028; QG37_00967.
DR VEuPathDB; FungiDB:B9J08_003761; -.
DR VEuPathDB; FungiDB:CJI96_0002292; -.
DR VEuPathDB; FungiDB:CJI97_003833; -.
DR VEuPathDB; FungiDB:CJJ07_003661; -.
DR VEuPathDB; FungiDB:CJJ09_000347; -.
DR VEuPathDB; FungiDB:QG37_00967; -.
DR Proteomes; UP000037122; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0031422; C:RecQ family helicase-topoisomerase III complex; IEA:EnsemblFungi.
DR GO; GO:0035861; C:site of double-strand break; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:EnsemblFungi.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:EnsemblFungi.
DR GO; GO:0043007; P:maintenance of rDNA; IEA:EnsemblFungi.
DR GO; GO:1902969; P:mitotic DNA replication; IEA:EnsemblFungi.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:EnsemblFungi.
DR GO; GO:0006301; P:postreplication repair; IEA:EnsemblFungi.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IEA:EnsemblFungi.
DR GO; GO:0000018; P:regulation of DNA recombination; IEA:EnsemblFungi.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW DNA-binding; Isomerase; Magnesium; Metal-binding; Topoisomerase.
FT CHAIN 1..640
FT /note="DNA topoisomerase 3"
FT /id="PRO_0000447629"
FT DOMAIN 21..175
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
SQ SEQUENCE 640 AA; 72613 MW; 7BAF8ACE9A8FE904 CRC64;
MLISTLPLLL HEQLAQSTRM RVLCVAEKNS IAKEVAKILS GGRARPRNSL YKYVKNYDFQ
YTFQGLGPCD VTMTAVAGHV LTTDFGPEYA WGKCPPGRLF DAPFLTKPPP DRDQRAGILK
NIIREARNAD RLMIWTDCDR EGEYIGWEIM SVAQGANPRL NLQTTWRAQF SHLEPQHIVA
AANNPKALDM KLVAAVECRT EFDLRVGTLF TRFLTNIYKS KRLVGEKEVV SYGTCQFPTL
SFVVDRYVRV RNFRPEPFWS IDLAVTKNGQ KVNFSWSRNH LFDRMFVYVI YAQLLEGPQK
PRIVGVSTKP TSHYKPLPLT TVDLQKCCSR YFKMLAKAAL DAAELLYTAG YISYPRTETD
QFPAKLDLKG YITKQTLSLD WGTHATRLLQ GSFRPPRGGK HDDKAHPPIY PVKSASLDTL
RPDQRKVYEF VVRRFLACCS DDARGLQTKV DLQWRSERFT ALGLQVTERN FLDVYPYSDW
KSLAQLPEFA EGEEVTPSSC KVKEGKTSPP NYMTEAELIA LMDANGIGTD ATIADHVEKI
AQRNYVTRRK IGKSEVFIPT SLGISLIDAF DAILIDRISL LKPFLRRAME GFLQKISRGE
ITKQDVISQL LPLYKEAFME SNQKGHVISD TFIQTSRGLS
