ID   TOP6B_ORYSJ             Reviewed;         696 AA.
AC   Q6H442; A0A0P0XKM8; Q6UFU6;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=DNA topoisomerase 6 subunit B;
DE            Short=OsTOP6B;
DE            EC=5.6.2.2;
GN   Name=TOP6B; OrderedLocusNames=Os09g0279600, LOC_Os09g10770;
GN   ORFNames=OsJ_28656, P0651G05.4;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Zhonghua 10; TISSUE=Flower;
RA   Wang T., Ding Z.J.;
RT   "Molecular characterization of OsTOP6B, a homolog of subunit B of
RT   archaebacterial topoisomerase 6, from Oryza sativa.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
RP   HOMODIMERIZATION, AND INTERACTION WITH SPO11-4.
RC   STRAIN=cv. Zhonghua 10;
RX   PubMed=21637817; DOI=10.1371/journal.pone.0020327;
RA   An X.J., Deng Z.Y., Wang T.;
RT   "OsSpo11-4, a rice homologue of the archaeal TopVIA protein, mediates
RT   double-strand DNA cleavage and interacts with OsTopVIB.";
RL   PLoS ONE 6:E20327-E20327(2011).
CC   -!- FUNCTION: Component of the DNA topoisomerase VI involved in chromatin
CC       organization and progression of endoreduplication cycles. Relaxes both
CC       positive and negative superturns and exhibits a strong decatenase
CC       activity. The B subunit binds ATP (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2;
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two TOP6A and two TOP6B subunits
CC       (Probable). Interacts with SPO11-4. {ECO:0000269|PubMed:21637817,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TOP6B family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ75096.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY371050; AAQ75096.1; ALT_FRAME; mRNA.
DR   EMBL; AP006528; BAD26507.1; -; Genomic_DNA.
DR   EMBL; AP008215; BAF24675.1; -; Genomic_DNA.
DR   EMBL; AP014965; BAT07216.1; -; Genomic_DNA.
DR   EMBL; CM000146; EEE69338.1; -; Genomic_DNA.
DR   EMBL; AK101452; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015612693.1; XM_015757207.1.
DR   AlphaFoldDB; Q6H442; -.
DR   SMR; Q6H442; -.
DR   STRING; 4530.OS09T0279600-01; -.
DR   PaxDb; Q6H442; -.
DR   PRIDE; Q6H442; -.
DR   EnsemblPlants; Os09t0279600-01; Os09t0279600-01; Os09g0279600.
DR   GeneID; 4346606; -.
DR   Gramene; Os09t0279600-01; Os09t0279600-01; Os09g0279600.
DR   KEGG; osa:4346606; -.
DR   eggNOG; ENOG502QQC0; Eukaryota.
DR   HOGENOM; CLU_006403_1_0_1; -.
DR   InParanoid; Q6H442; -.
DR   OMA; TRIELEM; -.
DR   OrthoDB; 545371at2759; -.
DR   Proteomes; UP000000763; Chromosome 9.
DR   Proteomes; UP000007752; Chromosome 9.
DR   Proteomes; UP000059680; Chromosome 9.
DR   Genevisible; Q6H442; OS.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
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:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:EnsemblPlants.
DR   GO; GO:0042023; P:DNA endoreduplication; IEA:EnsemblPlants.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0007389; P:pattern specification process; IEA:EnsemblPlants.
DR   GO; GO:0009741; P:response to brassinosteroid; IEA:EnsemblPlants.
DR   GO; GO:0010026; P:trichome differentiation; IEA:EnsemblPlants.
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; 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; PF09239; Topo-VIb_trans; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA-binding; Isomerase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Topoisomerase.
FT   CHAIN           1..696
FT                   /note="DNA topoisomerase 6 subunit B"
FT                   /id="PRO_0000429781"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         208..209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         217..224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         543
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        417
FT                   /note="F -> I (in Ref. 6; AK101452)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   696 AA;  78015 MW;  86958776B4EE6DD2 CRC64;
     MDDDAGDGAA SGGTKRKVTA ASSSAAAKGK AAGKGKAASK ASALATAKES SLLKQKSPAE
     FFAENKNIAG FDNPGKSLYT TMRELVENAL DSAESISELP DIEIIIEEIT KSKFNTMIGL
     VDRQRIDEEL YDDFESAKAR EKRLAKEARF QETQAKNAAL GKKVKEAPAA RGKGRGEAAF
     FRVTCKDNGR GMPHDDIPNM LGRVLSGTKY GLRQTRGKFG LGAKMALIWS KMSTGLPIEI
     KSSMKGQNFI SFCLLDIDIH KNVPHVHLHE KRENKDRWHG AELQVIIEGN WTTHRSKILH
     YMRQMAVITP YAQFLFRFLS DSPDKNLTIQ FARRTDVMPP IPLQTKHHPS AVDLLLIKRL
     ISETTKQNLL QFLQHEFVNI SKSHAERLIG EMGPDFSAKT TVKSLTSQQL VRIHQLFRQA
     KFDDPSGNCL SPAGEYNLRL GIIKELHPDL VATHASSPQV FEGHPFIVEA GISIGGKDVK
     HGLNIFRYAN RIPLLFEQGA DVITRTALKR INWSSYKINQ QQDKIGVFVS IVSTKIPFKG
     TGKEYIGDDI TEIASAVQSA LKQCCLQLKS KIVKKLQARE RQDRKRNLNR YIPDVARAIM
     ETLGEIADES PPKRPRYDKE DEELLEKVNS EEVTEMTFRD CLTQHVEQVD YEMALEYAMQ
     SGVSEEPREA LYLNSLEGSY KFIDFQSPVF VFRFIP