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Database: UniProt
Entry: I3R524_HALMT
LinkDB: I3R524_HALMT
Original site: I3R524_HALMT 
ID   I3R524_HALMT            Unreviewed;       366 AA.
AC   I3R524;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 78.
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   ECO:0000313|EMBL:AFK19334.1};
GN   OrderedLocusNames=HFX_1628 {ECO:0000313|EMBL:AFK19334.1};
GN   ORFNames=BM92_00965 {ECO:0000313|EMBL:AHZ21310.1}, C439_02332
GN   {ECO:0000313|EMBL:EMA04475.1}, E6P09_11180
GN   {ECO:0000313|EMBL:QCQ75803.1};
OS   Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS   14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK19334.1, ECO:0000313|Proteomes:UP000006469};
RN   [1] {ECO:0000313|EMBL:AFK19334.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.2087 {ECO:0000313|EMBL:AFK19334.1};
RX   PubMed=22247127; DOI=10.1128/AEM.07114-11;
RA   Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
RT   "Identification of the haloarchaeal phasin (PhaP) that functions in
RT   polyhydroxyalkanoate accumulation and granule formation in Haloferax
RT   mediterranei.";
RL   Appl. Environ. Microbiol. 78:1946-1952(2012).
RN   [2] {ECO:0000313|EMBL:AFK19334.1, ECO:0000313|Proteomes:UP000006469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC   R-4 {ECO:0000313|Proteomes:UP000006469}, and CGMCC 1.2087
RC   {ECO:0000313|EMBL:AFK19334.1};
RX   PubMed=22843593; DOI=10.1128/JB.00880-12;
RA   Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA   Zhou J., Hu S., Xiang H.;
RT   "Complete genome sequence of the metabolically versatile halophilic
RT   archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT   hydroxyvalerate) producer.";
RL   J. Bacteriol. 194:4463-4464(2012).
RN   [3] {ECO:0000313|Proteomes:UP000011603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC   R-4 {ECO:0000313|Proteomes:UP000011603};
RA   Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA   Eisen J.A., Facciotti M.T.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:EMA04475.1, ECO:0000313|Proteomes:UP000011603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 {ECO:0000313|EMBL:EMA04475.1}, and ATCC 33500 / DSM
RC   1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC   {ECO:0000313|Proteomes:UP000011603};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [5] {ECO:0000313|EMBL:AHZ21310.1, ECO:0000313|Proteomes:UP000027075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 {ECO:0000313|EMBL:AHZ21310.1}, and ATCC 33500 / DSM
RC   1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC   {ECO:0000313|Proteomes:UP000027075};
RA   Bautista V.;
RT   "Transcriptional profiles of Haloferax mediterranei on the basis of
RT   nitrogen availability.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:AFK19334.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.2087;
RA   Wang L., Yang H., Xiang H.;
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:QCQ75803.1, ECO:0000313|Proteomes:UP000299011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 {ECO:0000313|EMBL:QCQ75803.1}, and ATCC 33500 / DSM
RC   1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC   {ECO:0000313|Proteomes:UP000299011};
RA   DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA   Roberts R.J.;
RT   "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT   mediterranei.";
RL   Submitted (APR-2019) 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; CP001868; AFK19334.1; -; Genomic_DNA.
DR   EMBL; CP007551; AHZ21310.1; -; Genomic_DNA.
DR   EMBL; AOLO01000002; EMA04475.1; -; Genomic_DNA.
DR   EMBL; CP039139; QCQ75803.1; -; Genomic_DNA.
DR   RefSeq; WP_004056801.1; NZ_CP039139.1.
DR   AlphaFoldDB; I3R524; -.
DR   STRING; 523841.HFX_1628; -.
DR   PaxDb; 523841-HFX_1628; -.
DR   GeneID; 40156987; -.
DR   KEGG; hme:HFX_1628; -.
DR   PATRIC; fig|523841.21.peg.472; -.
DR   eggNOG; arCOG04143; Archaea.
DR   HOGENOM; CLU_037229_1_0_2; -.
DR   OrthoDB; 5866at2157; -.
DR   Proteomes; UP000006469; Chromosome.
DR   Proteomes; UP000011603; Unassembled WGS sequence.
DR   Proteomes; UP000027075; Chromosome.
DR   Proteomes; UP000299011; 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          72..138
FT                   /note="Spo11/DNA topoisomerase VI subunit A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04406"
FT   DOMAIN          142..191
FT                   /note="Type II DNA topoisomerase VI subunit A all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF20768"
FT   DOMAIN          194..360
FT                   /note="Topoisomerase 6 subunit A/Spo11 TOPRIM"
FT                   /evidence="ECO:0000259|Pfam:PF21180"
FT   ACT_SITE        101
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00132"
FT   BINDING         199
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00132"
FT   BINDING         251
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00132"
SQ   SEQUENCE   366 AA;  41879 MW;  5ADD87656EA03BA2 CRC64;
     MASESKTSEE LARERLMDLA AEFYDQFDAG EIPTMELPTR TKSNIEYDED ANVWVYGDRT
     STRSANSVRG ARKLLKAAYT IEFLARQLEE DRSSTLRELY YLSESWDAEE AHFSGQDESN
     QLIEDLEIVS EVTREDFHMR PEESGATLMG PLELREQTRR GERDIHCQLD VGEGGYQIPN
     NPDTIQFLDH DIDFVLCVET GGMRDRLIEN GFDEQYNVLI VHLKGQPARA TRRITKRLHD
     ELDLPVVVFT DGDPWSYRIY GSVAYGSIKS AHLSEYLATP EAKFIGIQPQ DIVDYDLPTD
     PLADSDINAL QSELEDPRFM TDYWKEQIEL QLDIGKKAEQ QALAARGLDF VTEEYLPTRL
     DEMGII
//
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