ID W1PNR1_AMBTC Unreviewed; 670 AA.
AC W1PNR1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=AMTR_s00022p00212920 {ECO:0000313|EMBL:ERN11652.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN11652.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
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}.
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DR EMBL; KI392687; ERN11652.1; -; Genomic_DNA.
DR RefSeq; XP_006850071.1; XM_006850008.2.
DR AlphaFoldDB; W1PNR1; -.
DR STRING; 13333.W1PNR1; -.
DR EnsemblPlants; ERN11652; ERN11652; AMTR_s00022p00212920.
DR GeneID; 18439852; -.
DR Gramene; ERN11652; ERN11652; AMTR_s00022p00212920.
DR KEGG; atr:18439852; -.
DR eggNOG; ENOG502QQC0; Eukaryota.
DR HOGENOM; CLU_006403_1_0_1; -.
DR OMA; VYRGNPF; -.
DR OrthoDB; 5487549at2759; -.
DR Proteomes; UP000017836; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000017836};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_03165}.
FT DOMAIN 400..557
FT /note="DNA topoisomerase VI subunit B transducer"
FT /evidence="ECO:0000259|Pfam:PF09239"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 539..597
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 16..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 183..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 192..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
SQ SEQUENCE 670 AA; 76148 MW; AF2F65111E59A736 CRC64;
MESNGSPELQ KSSKKRKGTS SQNPKSSVLK QKSPAEFFAE NKNIAGFDNP GKSLYTTVRE
LVENSLDSAE SISELPWIEI TIEEISKTKF NAMIGLIDRE RVDEELYDDF ETVKAREKRL
AKEARDQEIQ AKNIAHGKKI KETSKSTKSR GDASFFRVTC KDNGKGMPHE DIPNMFGRVL
SGTKYGLKQT RGKFGLGAKM ALIWSKMSTG LPIEILSSMR GQNYVSFCRL DIDIHRNIPH
VHIHEKRENK EEWHGAEIQV IIEGNWTTYR SKILHYMRQM AVITPYAQFL FKLISDMADK
NVTIHFARRT DVMPPVPVET KHHPSAVDLL LIKRLIAETS KQNLLQFLQH EFVNIRKSYA
ERLIGEMGSD FSPKMAVKSL SSQQVVRIHQ LFRQAKFADP SGDCLSPAGE YNLRLGIIKE
LHPDMVATYA GSPQVFEGHP FLIEAGVSLG GKDVKQGLNI FRFANRIPLL FEQGADVVTR
TAAKINWSCY KINQSQDKIG VFVSIVSTKI PFKGTGKEYI GADINEIVSA VKTSIQQCCI
QLKTKIVKKL QARERLERKR NLTRYIPDAS RAIYGVMKEI AKSRDSKQRQ YNEKEEEILN
KVSCREITEP IIKEKLTHYV EQVDYEMALE YAAQSGVSEE PREDIYISAL EGAPKFLDLH
HPVCVFRLFL
//
