ID C7NZR5_HALMD Unreviewed; 366 AA. AC C7NZR5; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAR-2024, entry version 83. 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 OrderedLocusNames=Hmuk_2727 {ECO:0000313|EMBL:ACV48833.1}; OS Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB OS 13541) (Haloarcula mukohataei). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales; OC Haloarculaceae; Halomicrobium. OX NCBI_TaxID=485914 {ECO:0000313|EMBL:ACV48833.1, ECO:0000313|Proteomes:UP000001746}; RN [1] {ECO:0000313|EMBL:ACV48833.1, ECO:0000313|Proteomes:UP000001746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541 RC {ECO:0000313|Proteomes:UP000001746}; RX PubMed=21304667; DOI=10.4056/sigs.42644; RA Tindall B.J., Schneider S., Lapidus A., Copeland A., Glavina Del Rio T., RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D., RA Goodwin L., Pitluck S., Mikhailova N., Pati A., Ivanova N., Mavrommatis K., RA Chen A., Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J., RA Jeffries C.D., Brettin T., Han C., Rohde M., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C., RA Detter J.C.; RT "Complete genome sequence of Halomicrobium mukohataei type strain (arg- RT 2)."; RL Stand. Genomic Sci. 1:270-277(2009). 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, ECO:0000256|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001688; ACV48833.1; -; Genomic_DNA. DR RefSeq; WP_015763675.1; NC_013202.1. DR AlphaFoldDB; C7NZR5; -. DR STRING; 485914.Hmuk_2727; -. DR GeneID; 8412278; -. DR KEGG; hmu:Hmuk_2727; -. DR eggNOG; arCOG04143; Archaea. DR HOGENOM; CLU_037229_1_0_2; -. DR OrthoDB; 5866at2157; -. DR Proteomes; UP000001746; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001746}; KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP- KW Rule:MF_00132}. FT DOMAIN 73..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; 41726 MW; 7CB5261BC4E2B5E1 CRC64; MSTDSNLNEA EAREQLLDLA ADFYDQFAEG DVPTMQIPTR TKSNIEYDED KDVWVYGDRS STRSAKTVSG AQKLLKATYT IDFLAQQLEE DRSSTLRELY YLSESWDLDE AQFNTQDESN NLIEDLEIVS EVKREDFHMR PEESGAKVMG PLLLREQTRR GDREIHCQDD VGQGGYQIPN NPDTIEFLDN DADFVLCVET GGMRDRLVEN GFDDEYDSIV VHLGGQPARA TRRLTKRLHD ELDLPVVVFT DGDPWSYRIY GSVAYGSIKS AHLSEYLATP EAQFIGIRPE DIVEYDLPTD PLSDSDINAL ESELEDPRFQ TEFWEEQIEL QLDIGKKSEQ QALASRGLDF VTDTYLPERL TEMGVL //