ID D8SDA0_SELML Unreviewed; 578 AA.
AC D8SDA0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=DNA topoisomerase 6 subunit B {ECO:0000256|HAMAP-Rule:MF_03165};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_03165};
GN Name=TOP6B {ECO:0000256|HAMAP-Rule:MF_03165};
GN ORFNames=SELMODRAFT_154417 {ECO:0000313|EMBL:EFJ17477.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ17477.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(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. {ECO:0000256|HAMAP-Rule:MF_03165}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03165};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two TOP6A and two TOP6B subunits.
CC {ECO:0000256|HAMAP-Rule:MF_03165}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03165}.
CC -!- SIMILARITY: Belongs to the TOP6B family. {ECO:0000256|HAMAP-
CC Rule:MF_03165}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03165}.
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DR EMBL; GL377613; EFJ17477.1; -; Genomic_DNA.
DR RefSeq; XP_002981289.1; XM_002981243.1.
DR AlphaFoldDB; D8SDA0; -.
DR STRING; 88036.D8SDA0; -.
DR EnsemblPlants; EFJ17477; EFJ17477; SELMODRAFT_154417.
DR GeneID; 9647556; -.
DR Gramene; EFJ17477; EFJ17477; SELMODRAFT_154417.
DR KEGG; smo:SELMODRAFT_154417; -.
DR eggNOG; ENOG502QQC0; Eukaryota.
DR HOGENOM; CLU_006403_1_0_1; -.
DR InParanoid; D8SDA0; -.
DR OMA; MIPMSIH; -.
DR OrthoDB; 5487549at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
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:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd00823; TopoIIB_Trans; 1.
DR Gene3D; 1.10.8.50; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00322; Top6B; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005734; TopoVI_B.
DR InterPro; IPR015320; TopoVI_B_transducer.
DR PANTHER; PTHR48356; DNA TOPOISOMERASE 6 SUBUNIT B; 1.
DR PANTHER; PTHR48356:SF1; DNA TOPOISOMERASE 6 SUBUNIT B; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF09239; Topo-VIb_trans; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF46946; S13-like H2TH domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03165};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_03165};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_03165};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03165}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03165};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_03165}.
FT DOMAIN 307..465
FT /note="DNA topoisomerase VI subunit B transducer"
FT /evidence="ECO:0000259|Pfam:PF09239"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 90..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 425
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
SQ SEQUENCE 578 AA; 64909 MW; EC0388654C601AA1 CRC64;
MIGLVDHERV DAELYDDYEN EKAREKRLAK EAREQERQAK AIAAGKKVTV PKAGKGRGDT
VFYKVSCKDN GKGMPHDDIP NMLGRVLSGT KYGLKQTRGK FGLGAKMALI WSKMSTGLPI
EISSAMKGQK FISFCRLDID IHKNIPNVHV LEKKPNTTGW HGAEIHVTIE GNWTTYRSKV
ISYMRQMAVI TPYAQFLFRY RAGTPEKNVS VQFVRRTDVM PPAPPETKYH PSAVDLLLIK
RLIAEKSKQT LIQYLQQDFV SINKSYAERL IGEMGPDFTP KMLVKDLTDQ QLVRIHQLFR
QAKFDDPDGD CLSPAGEYNL RLGITKELHP DMVATCQGNV QVFEGHPFIV EAAVSLGGKS
VKPGLNIFRF ANRIPLLFEQ GGDVITRTAT KRISWSAYKI SHLQDKVGVF VSIVSTKIPF
KGTGKEYIGD DITEIASGVK SAIQQCCIQL KAKLVRQKAA RDKLERKKNL SRYIPDVSRA
IYGVLASIAN EREAKRQKYE PDSREILHKV ADKEVTEVTL SRKLTQYVDQ VDAELALDYA
TQSGLVKARE PISLAGVDWN QANYLELHSP VCVMKLLS
//
