ID W8NTU9_9EURY Unreviewed; 384 AA.
AC W8NTU9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Type 2 DNA topoisomerase 6 subunit A {ECO:0000256|HAMAP-Rule:MF_00132};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00132};
DE AltName: Full=Type II DNA topoisomerase VI subunit A {ECO:0000256|HAMAP-Rule:MF_00132};
GN Name=top6A {ECO:0000256|HAMAP-Rule:MF_00132};
GN ORFNames=BD01_0948 {ECO:0000313|EMBL:AHL22567.1};
OS Thermococcus nautili.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=195522 {ECO:0000313|EMBL:AHL22567.1, ECO:0000313|Proteomes:UP000019434};
RN [1] {ECO:0000313|EMBL:AHL22567.1, ECO:0000313|Proteomes:UP000019434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30-1 {ECO:0000313|EMBL:AHL22567.1,
RC ECO:0000313|Proteomes:UP000019434};
RA Oberto J., Gaudin M., Cossu M., Gorlas A., Slesarev A., Marguet E.,
RA Forterre P.;
RT "Genome Sequence of an Hyperthermophilic Archaeon, Thermococcus nautili 30-
RT 1, producing viral vesicles.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Relaxes both positive and negative superturns and exhibits a
CC strong decatenase activity. {ECO:0000256|HAMAP-Rule:MF_00132}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185,
CC ECO:0000256|HAMAP-Rule:MF_00132};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00132};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two Top6A and two Top6B chains.
CC {ECO:0000256|HAMAP-Rule:MF_00132}.
CC -!- SIMILARITY: Belongs to the TOP6A family.
CC {ECO:0000256|ARBA:ARBA00006559, ECO:0000256|HAMAP-Rule:MF_00132}.
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DR EMBL; CP007264; AHL22567.1; -; Genomic_DNA.
DR RefSeq; WP_042690575.1; NZ_CP007264.1.
DR AlphaFoldDB; W8NTU9; -.
DR STRING; 195522.BD01_0948; -.
DR GeneID; 24958908; -.
DR KEGG; tnu:BD01_0948; -.
DR eggNOG; arCOG04143; Archaea.
DR HOGENOM; CLU_037229_1_0_2; -.
DR OrthoDB; 5866at2157; -.
DR Proteomes; UP000019434; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_00132; Top6A; 1.
DR InterPro; IPR002815; Spo11/TopoVI_A.
DR InterPro; IPR013049; Spo11/TopoVI_A_N.
DR InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR InterPro; IPR049333; Topo_VI_alpha.
DR InterPro; IPR004085; TopoVI_A.
DR InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10848; MEIOTIC RECOMBINATION PROTEIN SPO11; 1.
DR PANTHER; PTHR10848:SF0; MEIOTIC RECOMBINATION PROTEIN SPO11; 1.
DR Pfam; PF21180; TOP6A-Spo11_Toprim; 1.
DR Pfam; PF20768; Topo_VI_alpha; 1.
DR Pfam; PF04406; TP6A_N; 1.
DR PRINTS; PR01550; TOP6AFAMILY.
DR PRINTS; PR01552; TPISMRASE6A.
DR SUPFAM; SSF56726; DNA topoisomerase IV, alpha subunit; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00132};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00132};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00132};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00132};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00132};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00132};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00132}.
FT DOMAIN 81..150
FT /note="Spo11/DNA topoisomerase VI subunit A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04406"
FT DOMAIN 157..193
FT /note="Type II DNA topoisomerase VI subunit A all-beta"
FT /evidence="ECO:0000259|Pfam:PF20768"
FT DOMAIN 199..377
FT /note="Topoisomerase 6 subunit A/Spo11 TOPRIM"
FT /evidence="ECO:0000259|Pfam:PF21180"
FT ACT_SITE 110
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00132"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00132"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00132"
SQ SEQUENCE 384 AA; 44272 MW; A5A4A07E9A15DDD6 CRC64;
MPKAIKRERP KEKFSYDPKK VLSKLEEYGR SVLEAIKAGK NPYFDIPTRG LNNVYFDEKS
RLIKMGDKLS RRYFLNVAHA RKFMQTLLIM AYVKRLVAEG KHASLREAYY ANKHTIPGTK
ENTFEDQRES DPIIEDLERM LGVLREEMHI TADRRGYIYG DIVIRDGEDE FNASKLGSGG
WAVPGTVEHI QFPEINVDYA LVVETAAMAD RLIEEKFPKK EKALIIATQG QASRGVRRLI
HRLHYEEGLP IIVFTDGDPY GWYIYSTIKQ GSINLAYLSD KLATPEARFV GMTMDDIKRY
GLENVTEKLK GIPPNKKGGP TGDYKRILEE MEYPWFQNKE WQRQLKMALK WGVRIEQQAL
ANKSLEFVAK EYLPEKINNG DLLP
//
