TOP6A_HALS3
ID TOP6A_HALS3 Reviewed; 366 AA.
AC B0R4D2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Type 2 DNA topoisomerase 6 subunit A {ECO:0000255|HAMAP-Rule:MF_00132};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00132};
DE AltName: Full=Type II DNA topoisomerase VI subunit A {ECO:0000255|HAMAP-Rule:MF_00132};
GN Name=top6A {ECO:0000255|HAMAP-Rule:MF_00132}; OrderedLocusNames=OE_2301R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
CC -!- FUNCTION: Relaxes both positive and negative superturns and exhibits a
CC strong decatenase activity. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00132};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00132};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two Top6A and two Top6B chains.
CC {ECO:0000255|HAMAP-Rule:MF_00132}.
CC -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000255|HAMAP-
CC Rule:MF_00132}.
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DR EMBL; AM774415; CAP13597.1; -; Genomic_DNA.
DR RefSeq; WP_010902622.1; NC_010364.1.
DR AlphaFoldDB; B0R4D2; -.
DR SMR; B0R4D2; -.
DR EnsemblBacteria; CAP13597; CAP13597; OE_2301R.
DR GeneID; 5952734; -.
DR GeneID; 62886452; -.
DR KEGG; hsl:OE_2301R; -.
DR HOGENOM; CLU_037229_1_0_2; -.
DR OMA; NWGEARF; -.
DR PhylomeDB; B0R4D2; -.
DR Proteomes; UP000001321; 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; 1.10.10.10; -; 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; IPR004085; TopoVI_A.
DR InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10848; PTHR10848; 1.
DR Pfam; PF04406; TP6A_N; 1.
DR PRINTS; PR01550; TOP6AFAMILY.
DR PRINTS; PR01552; TPISMRASE6A.
DR SUPFAM; SSF56726; SSF56726; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Topoisomerase.
FT CHAIN 1..366
FT /note="Type 2 DNA topoisomerase 6 subunit A"
FT /id="PRO_1000095768"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
SQ SEQUENCE 366 AA; 41449 MW; 21B08189088E768F CRC64;
MSETHTSDET EARDQLLAIA EQFYDQFADG DIPRMSLPTR SKSNIEYDED ADVWVYGDSQ
STRSANSVRG ARKLLKSVYT VDFLAQQLDE GRSSTLRELY YLSESWDEAE AQFNDQSESD
KLVEDLEIVS GVKREDFHMR PEESGAKVMG PLRLREQTRR GDREIHCQED VGQGGYQIPN
NPDTIDFLDT DADFVLCVET GGMRDRLVEN GFDDDYNAIV VHLGGQPARA TRRLTKRLHD
ELDLPVTVFT DGDPWSYRIY GSVAYGSIKS AHLSEYLATP QAQFIGIRPQ DIVDYDLPTD
PLSDSDVNAL ESELEDPRFQ SDFWTEQIGL QLDIDKKAEQ QALASRGLDF VTDTYLPERL
AEMGVL