ID A0A022S227_ERYGU Unreviewed; 674 AA.
AC A0A022S227;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=MIMGU_mgv1a002442mg {ECO:0000313|EMBL:EYU46311.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU46311.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU46311.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(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; KI630171; EYU46311.1; -; Genomic_DNA.
DR RefSeq; XP_012829980.1; XM_012974526.1.
DR AlphaFoldDB; A0A022S227; -.
DR STRING; 4155.A0A022S227; -.
DR GeneID; 105951136; -.
DR KEGG; egt:105951136; -.
DR eggNOG; ENOG502QQC0; Eukaryota.
DR OMA; VYRGNPF; -.
DR OrthoDB; 5487549at2759; -.
DR PhylomeDB; A0A022S227; -.
DR Proteomes; UP000030748; 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:UP000030748};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_03165}.
FT DOMAIN 403..562
FT /note="DNA topoisomerase VI subunit B transducer"
FT /evidence="ECO:0000259|Pfam:PF09239"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 186..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 195..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
SQ SEQUENCE 674 AA; 76046 MW; 8BBA1DE85BA77B3F CRC64;
MEVGGSSESP SETKKSKSKT PRKTKDAAQT LKQKSPAEFF ADNKNIAGFD NPGKCLYTTV
RELVENALDS AESIAELPII EITIEEIGKN QYNSMIGLAD HGRVDEALYD DFETVKAREK
RLAKEARIQE NQAKSAALGK KGKAATAVKP IKSRETSYYR VSCKDNGRGM PHDDIPNMFG
RVLSGTKYGL KQTRGKYGLG AKMALIWSKM STGLPIEILS SMKGQSYSSF CRLDIDINKN
IPHIHVHEKR KNEERWHGAE IQIVIEGNWT TYRSKILHYM RQMAVITPYS QFLFKFLSGS
PDKNVTVRFA RRTDIMPPAP LETKYHPSAV DLLLIKRLIT ETSKQNLLQF LQHEFVNVGK
SHAERLIGEM GTDFSPKMAV KSLTSQQIVR IHQLFRQAKF DDPSGDCLSP AGEYNLRLGI
IKELHPDMVA TYSGSAQVFE GHPFIVEAGL SLGGKDVKQG LNIFRFANRI PLLFEQGADV
VTRTAAKRIN WNNYKINQTQ DKIGVFVSIV STKIPFKGTG KEYIGDDISE IASAVKTAIQ
QCCSQLKSKI VKRIQAREQQ ERKRSLNKYI PNATTAIYDI LKEMSRAHAS KKRRYDGKDA
ELLKQVSAQL VTQETLREKL AQHVEQVDYE MAMEYATQTG VNEEPREEIY IPPLEAQCSF
TEFHSPIFVF RLFN
//
