ID   TOP6B_PYRFU             Reviewed;         568 AA.
AC   Q8U0K8;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Type 2 DNA topoisomerase 6 subunit B {ECO:0000255|HAMAP-Rule:MF_00322};
DE            EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00322};
DE   AltName: Full=Type II DNA topoisomerase VI subunit B {ECO:0000255|HAMAP-Rule:MF_00322};
DE            Short=TopoVI-B {ECO:0000255|HAMAP-Rule:MF_00322};
GN   Name=top6B {ECO:0000255|HAMAP-Rule:MF_00322}; OrderedLocusNames=PF1579;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
CC   -!- FUNCTION: Relaxes both positive and negative superturns and exhibits a
CC       strong decatenase activity. {ECO:0000255|HAMAP-Rule:MF_00322}.
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_00322};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two Top6A and two Top6B chains.
CC       {ECO:0000255|HAMAP-Rule:MF_00322}.
CC   -!- SIMILARITY: Belongs to the TOP6B family. {ECO:0000255|HAMAP-
CC       Rule:MF_00322}.
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DR   EMBL; AE009950; AAL81703.1; -; Genomic_DNA.
DR   RefSeq; WP_011012725.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U0K8; -.
DR   SMR; Q8U0K8; -.
DR   IntAct; Q8U0K8; 1.
DR   STRING; 186497.PF1579; -.
DR   PRIDE; Q8U0K8; -.
DR   EnsemblBacteria; AAL81703; AAL81703; PF1579.
DR   GeneID; 41713403; -.
DR   KEGG; pfu:PF1579; -.
DR   PATRIC; fig|186497.12.peg.1645; -.
DR   eggNOG; arCOG01165; Archaea.
DR   HOGENOM; CLU_006403_0_0_2; -.
DR   OMA; TRIELEM; -.
DR   OrthoDB; 13565at2157; -.
DR   PhylomeDB; Q8U0K8; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00823; TopoIIB_Trans; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   HAMAP; MF_00322; Top6B; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005734; TopoVI_B.
DR   InterPro; IPR015320; TopoVI_B_transducer.
DR   PANTHER; PTHR10871:SF4; PTHR10871:SF4; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF09239; Topo-VIb_trans; 1.
DR   PIRSF; PIRSF006553; TopoVI_B; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR01052; top6b; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Isomerase; Nucleotide-binding;
KW   Reference proteome; Topoisomerase.
FT   CHAIN           1..568
FT                   /note="Type 2 DNA topoisomerase 6 subunit B"
FT                   /id="PRO_0000145467"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         99..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         109..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
FT   BINDING         473
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00322"
SQ   SEQUENCE   568 AA;  64429 MW;  6240A450DBAFE9FB CRC64;
     MAEARDLFKE FKVQSVSEFF RRNAAMLGYT GSIRSLTTVI HEAVTNSLDA CEEAGILPYV
     RVEIEELGKE HYKVIVEDNG PGIPEDYIPH VFGKMLAGTK AHRNIQSRGQ QGIGISGAVM
     FAQITSGKAT RVITSTGDDE IVEAWVKIDV QKNEGKIVKK IKHPNPKRWR GTRIELEVKN
     VKYVRSKQGV YWYLKLTAIA NPHAHIELVE PDGKLIVFPR SSEDIPEPPV EMKPHPKGVM
     TDDVYTMAHR SKRSTVRRFL VSEFSRISDK KVDELVLYIA ALRLINREVT DQNLKSQLIE
     RLANGEVEKV LKSFGRKWKK VVEEVEKIME KPPEKLTWHE AEEIVEAFKL MKFLAPPTYG
     LRPIGEENIE KGLSSILRPE FVTAVTRPPK VYSGGIPFQV EVGIAYGGEI TNSEILRYAN
     RVPLLFDAGS CVITSAVRSI DWRRYRVESF DNAPLVVLVN VVSVHVPYTS TGKQSIASID
     EIYNEIRLAL MEAARRLAAY LGGKYRRLYQ IRRKKIFEKY LPEIARSLHI LTGEPEEKIK
     EYFLRLIESK ITVAQEGVSE VEVEEGEA