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Database: UniProt
Entry: K0B5I7_9ARCH
LinkDB: K0B5I7_9ARCH
Original site: K0B5I7_9ARCH 
ID   K0B5I7_9ARCH            Unreviewed;       370 AA.
AC   K0B5I7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
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=NKOR_07760 {ECO:0000313|EMBL:AFS81413.1};
OS   Candidatus Nitrosopumilus koreensis AR1.
OC   Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC   Nitrosopumilaceae; Nitrosopumilus.
OX   NCBI_TaxID=1229908 {ECO:0000313|EMBL:AFS81413.1, ECO:0000313|Proteomes:UP000006101};
RN   [1] {ECO:0000313|EMBL:AFS81413.1, ECO:0000313|Proteomes:UP000006101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR1 {ECO:0000313|EMBL:AFS81413.1,
RC   ECO:0000313|Proteomes:UP000006101};
RX   PubMed=23209206; DOI=10.1128/JB.01857-12;
RA   Park S.J., Kim J.G., Jung M.Y., Kim S.J., Cha I.T., Kwon K., Lee J.H.,
RA   Rhee S.K.;
RT   "Draft Genome Sequence of an Ammonia-Oxidizing Archaeon, "Candidatus
RT   Nitrosopumilus koreensis" AR1, from Marine Sediment.";
RL   J. Bacteriol. 194:6940-6941(2012).
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; CP003842; AFS81413.1; -; Genomic_DNA.
DR   RefSeq; WP_014963792.1; NC_018655.1.
DR   AlphaFoldDB; K0B5I7; -.
DR   STRING; 1229908.NKOR_07760; -.
DR   GeneID; 13724391; -.
DR   KEGG; nkr:NKOR_07760; -.
DR   PATRIC; fig|1229908.8.peg.1685; -.
DR   HOGENOM; CLU_037229_1_0_2; -.
DR   Proteomes; UP000006101; 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; 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; 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|HAMAP-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}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00132};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_00132}.
FT   DOMAIN          82..146
FT                   /note="Spo11/DNA topoisomerase VI subunit A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04406"
FT   DOMAIN          200..364
FT                   /note="Topoisomerase 6 subunit A/Spo11 TOPRIM"
FT                   /evidence="ECO:0000259|Pfam:PF21180"
FT   ACT_SITE        111
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   370 AA;  42083 MW;  46D31C4EF43AB1E0 CRC64;
     MKTNKEKAKE ISKKAKEKQK SVLESLKNHG AKIYEDLENG RFPKFSIPSR SVGNIVYDKK
     LRQYILGNSN ALRSAKNSAQ LRSFTQLMWL AFFANRLTQE KKSSTLRDVY YSSQAFAIEF
     EDQSESDNII VDLEAVTSRP REDFHIFPEE RSSIFGDLNI EYTIPGYEGK KMNLSNHPDG
     YSIGPSLTTA ELVDTSAEIV IAIEKGGLFT RFVEEQIDKK FKSIIINTGG QAPRSTRTLL
     KRLHDELGLP VIILTDGDVY GEHIAMVIKS GSANAAHLRE LTVPDAKWVG VWATDIEKYK
     LPTIPMTESD IKRCYDLQKD PRYESGIWKK ELEVFLRLKR KAELEAFAKY GLTNITDKYL
     PQKLELAKSL
//
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