ID   TOP6A_METAC             Reviewed;         373 AA.
AC   Q8TQF8;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 111.
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=MA_1586;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM04999.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE010299; AAM04999.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048065160.1; NC_003552.1.
DR   AlphaFoldDB; Q8TQF8; -.
DR   SMR; Q8TQF8; -.
DR   STRING; 188937.MA_1586; -.
DR   EnsemblBacteria; AAM04999; AAM04999; MA_1586.
DR   GeneID; 1473474; -.
DR   KEGG; mac:MA_1586; -.
DR   HOGENOM; CLU_037229_1_0_2; -.
DR   InParanoid; Q8TQF8; -.
DR   OMA; NWGEARF; -.
DR   OrthoDB; 22842at2157; -.
DR   PhylomeDB; Q8TQF8; -.
DR   Proteomes; UP000002487; 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; IBA:GO_Central.
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; Reference proteome; Topoisomerase.
FT   CHAIN           1..373
FT                   /note="Type 2 DNA topoisomerase 6 subunit A"
FT                   /id="PRO_0000145448"
FT   ACT_SITE        110
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT   BINDING         206
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT   BINDING         258
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
SQ   SEQUENCE   373 AA;  42529 MW;  A9B29B2268214216 CRC64;
     MAGDVNNEVN SKKRQGDTLA KERLLGLAEK IYNQFEEEVI PSVSLPSRTK ANIEYSDESD
     VWVYGDRESE RSAKTVKGAF QLLKTTYATD FLINEHLAHN RGSTLRELYY ISEGWDYAKF
     KEQAESDRLI EDLELLTSLQ REYFHMRPEE DGATMFGPIE ISELTKRGAR NIHCQKDVGE
     GGYQIPFNVE NIEFKNHDAS MIIAIETGGM YARLMENGFD EAYNAILVHL KGQPARSTRR
     IIKRMNEELE IPVAVFTDGD PWSYRIYASV AYGAIKSAHL SEFMATPAAR FLGLQPSDIV
     EYELSTDKLT EQDISALRSE LSDPRFESEY WKEQIQLQLD IGKKAEQQAF AGKGLDFVTE
     VYLPNRLKEL GMV