TOP6B_ARATH
ID TOP6B_ARATH Reviewed; 670 AA.
AC Q9C5V6; Q9LT43;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=DNA topoisomerase 6 subunit B {ECO:0000255|HAMAP-Rule:MF_03165};
DE Short=AtTOP6B;
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_03165};
DE AltName: Full=Protein BRASSINOSTEROID INSENSITIVE 3;
DE AltName: Full=Protein ELONGATED HYPOCOTYL 6;
DE AltName: Full=Protein ROOT HAIRLESS 3;
GN Name=TOP6B {ECO:0000255|HAMAP-Rule:MF_03165}; Synonyms=BIN3, HYP6, RHL3;
GN OrderedLocusNames=At3g20780; ORFNames=MOE17.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH TOP6A;
RP SPO11-1 AND SPO11-2.
RX PubMed=11410368; DOI=10.1016/s0378-1119(01)00496-6;
RA Hartung F., Puchta H.;
RT "Molecular characterization of homologues of both subunits A (SPO11) and B
RT of the archaebacterial topoisomerase 6 in plants.";
RL Gene 271:81-86(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12119417; DOI=10.1073/pnas.152337599;
RA Yin Y., Cheong H., Friedrichsen D., Zhao Y., Hu J., Mora-Garcia S.,
RA Chory J.;
RT "A crucial role for the putative Arabidopsis topoisomerase VI in plant
RT growth and development.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10191-10196(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=12401175; DOI=10.1016/s0960-9822(02)01198-3;
RA Sugimoto-Shirasu K., Stacey N.J., Corsar J., Roberts K., McCann M.C.;
RT "DNA topoisomerase VI is essential for endoreduplication in Arabidopsis.";
RL Curr. Biol. 12:1782-1786(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INTERACTION WITH RHL1.
RX PubMed=16339310; DOI=10.1073/pnas.0505883102;
RA Sugimoto-Shirasu K., Roberts G.R., Stacey N.J., McCann M.C., Maxwell A.,
RA Roberts K.;
RT "RHL1 is an essential component of the plant DNA topoisomerase VI complex
RT and is required for ploidy-dependent cell growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18736-18741(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [7]
RP INTERACTION WITH BIN4.
RX PubMed=18055605; DOI=10.1105/tpc.107.054833;
RA Breuer C., Stacey N.J., West C.E., Zhao Y., Chory J., Tsukaya H., Azumi Y.,
RA Maxwell A., Roberts K., Sugimoto-Shirasu K.;
RT "BIN4, a novel component of the plant DNA topoisomerase VI complex, is
RT required for endoreduplication in Arabidopsis.";
RL Plant Cell 19:3655-3668(2007).
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. Involved in cell-elongation
CC processes. {ECO:0000255|HAMAP-Rule:MF_03165,
CC ECO:0000269|PubMed:12119417, ECO:0000269|PubMed:12401175}.
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_03165};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two TOP6A and two TOP6B subunits.
CC Interacts with SPO11-2, but not with SPO11-1, RHL1 or BIN4.
CC {ECO:0000255|HAMAP-Rule:MF_03165, ECO:0000269|PubMed:11410368,
CC ECO:0000269|PubMed:16339310, ECO:0000269|PubMed:18055605}.
CC -!- INTERACTION:
CC Q9C5V6; Q9LZ03: TOP6A; NbExp=7; IntAct=EBI-1772132, EBI-1772104;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03165}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves, stems, flowers and
CC seedlings. {ECO:0000269|PubMed:11410368}.
CC -!- DISRUPTION PHENOTYPE: Plants are defective in cell elongation and show
CC a severe dwarf phenotype. {ECO:0000269|PubMed:12119417}.
CC -!- SIMILARITY: Belongs to the TOP6B family. {ECO:0000255|HAMAP-
CC Rule:MF_03165}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02486.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ297843; CAC24690.1; -; mRNA.
DR EMBL; AB025629; BAB02486.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76422.1; -; Genomic_DNA.
DR RefSeq; NP_188714.2; NM_112969.3.
DR AlphaFoldDB; Q9C5V6; -.
DR SMR; Q9C5V6; -.
DR DIP; DIP-40170N; -.
DR IntAct; Q9C5V6; 2.
DR STRING; 3702.AT3G20780.1; -.
DR PaxDb; Q9C5V6; -.
DR PRIDE; Q9C5V6; -.
DR ProteomicsDB; 234444; -.
DR EnsemblPlants; AT3G20780.1; AT3G20780.1; AT3G20780.
DR GeneID; 821626; -.
DR Gramene; AT3G20780.1; AT3G20780.1; AT3G20780.
DR KEGG; ath:AT3G20780; -.
DR Araport; AT3G20780; -.
DR TAIR; locus:2091916; AT3G20780.
DR eggNOG; ENOG502QQC0; Eukaryota.
DR HOGENOM; CLU_006403_1_0_1; -.
DR InParanoid; Q9C5V6; -.
DR OMA; TRIELEM; -.
DR OrthoDB; 545371at2759; -.
DR PhylomeDB; Q9C5V6; -.
DR PRO; PR:Q9C5V6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C5V6; baseline and differential.
DR Genevisible; Q9C5V6; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; ISS:TAIR.
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; ISS:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
DR GO; GO:0000902; P:cell morphogenesis; IMP:TAIR.
DR GO; GO:0042023; P:DNA endoreduplication; IMP:TAIR.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0007389; P:pattern specification process; IMP:TAIR.
DR GO; GO:0009741; P:response to brassinosteroid; IMP:TAIR.
DR GO; GO:0010026; P:trichome differentiation; IMP:TAIR.
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 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..670
FT /note="DNA topoisomerase 6 subunit B"
FT /id="PRO_0000346112"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03165"
FT BINDING 160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03165"
FT BINDING 181..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03165"
FT BINDING 190..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03165"
FT BINDING 516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03165"
SQ SEQUENCE 670 AA; 75852 MW; 5735F0A6B4578D61 CRC64;
MAGDDLVETK KGSSKNSKDS NESKLKQKSP AEFFAENKNI AGFDNPGKSL YTTVRELVEN
ALDSAESISE LPEVEVTIEE IVKSKFNSMI GLIDRERVDT QLYDDYETEK ARGKRLAKEA
RASEIQAKNL ASGKKNKEPG VSKVLKARGE ASYYKVTCKD NGKGMPHDDI PNMFGRVLSG
TKYGLKQTRG KFGLGAKMAL IWSKMSTGLP IEISSSMKSQ NYVTFCRLDI DIHRNIPHIH
LHEKKGNKEK WHGAEIQVVI EGNWTTYRSK ILHYMRQMAV ITPYAQFLFR FISETPEKNV
TIKFTRRTDV MPPIPIETKH HPSSVDLLLI KRLITDTSKK TLLQFLQNEF VNINKTLAAR
LIGEMGPDFG PSMAVKSVTS QQMVRIHQLF RQAKFDDPSG DCLSPAGEYN LRLGIIKELH
PDMVATYSGS AQVFEGHPFI VEAGVSLGGR DVKQGINIFR FANRIPLLFE QGADVVTRTA
LKRINWNSYK INQTQDKIGV FVSIVSTKIP FKGTGKEYIG DDISEIATAV KSAIQQCCIQ
LKSKIVKRLQ AREQQERKRS LSRYIPDATG AVYEVLKQMT EEHKTKRKRY GEEDIVMLDK
VSKQIITKET LKEKLAEHVE QVDYEMALEY ATQSGVSEEP RENIYLQHLD PNKSNFIDLH
SPTFVFRLML
