ID A0A250WTD7_9CHLO Unreviewed; 1401 AA.
AC A0A250WTD7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=CEUSTIGMA_g1449.t1 {ECO:0000313|EMBL:GAX73999.1};
OS Chlamydomonas eustigma.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX73999.1, ECO:0000313|Proteomes:UP000232323};
RN [1] {ECO:0000313|EMBL:GAX73999.1, ECO:0000313|Proteomes:UP000232323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX73999.1,
RC ECO:0000313|Proteomes:UP000232323};
RA Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT "Acidophilic green algal genome provides insights into adaptation to an
RT acidic environment.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAX73999.1}.
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DR EMBL; BEGY01000005; GAX73999.1; -; Genomic_DNA.
DR STRING; 1157962.A0A250WTD7; -.
DR OrthoDB; 5487549at2759; -.
DR Proteomes; UP000232323; Unassembled WGS sequence.
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: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 GO; GO:0006396; P:RNA processing; IEA:InterPro.
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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR HAMAP; MF_00322; Top6B; 1.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005734; TopoVI_B.
DR InterPro; IPR015320; TopoVI_B_transducer.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
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 Pfam; PF13428; TPR_14; 1.
DR SMART; SM00386; HAT; 5.
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; SSF48452; TPR-like; 2.
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:UP000232323};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_03165}.
FT DOMAIN 1124..1283
FT /note="DNA topoisomerase VI subunit B transducer"
FT /evidence="ECO:0000259|Pfam:PF09239"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 779
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 886
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 907..908
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 916..923
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
FT BINDING 1242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03165"
SQ SEQUENCE 1401 AA; 156252 MW; 29EBE3A6DD7EF8C9 CRC64;
MEYPPAVPPV ENGSLDPLNN PQDPNASTDN TTEAPPNPAL TKYHELWREV QAMPTDFNAW
TNLINAVEKL DDLEKVQTVY DTFLASYPLC YGYWKKYADA ELRLGSAARA AAVYERAVSA
TPYSVDIWMH YSAFHKELPE ATSDSMRGVF ERAVAAVGTD YLSHNIWNKY LAYEEEQGNK
LFLVALYTRL LGMPIRDLDK YYQGLKTLVS NASLLEVMTE EEASLIRSQL EEEQRQAAVE
TAAAKAKSEE EAAAAEAAQK AAESSAVDAP AEAKPADAVM TDADAVSAMD VAPGENPSSV
PAEPVATDVT ADSSAVAESS VPVESIPTAM VTEEDVKAGW MRSRDALYGM TAAELENRKL
FEELIKRSYF HVKPLDATQL TNWLKYLDYM EGKGDNVATM VLYERCLVPC ASYPEYWERY
IRWLEKHGLN EEAHAALQRA TITFCRSRPE IHLFAMHFDE RHGDVEGARK RYKHVLEELA
PRLLSATIAA ANFEKRHGNK EAACQLFELL MKEEQAKDDG ASKSTLPFLA MQYAQFLRVA
FKDYAKGRQV LHDALAVSPN KKQLWEAAIC YEEAVAADDM VKVVLELCER ASAPQGVTAQ
EGKPVANLPD KDREDFSLKA IEFADAHGSM ADLLEAERRH AANFLVPSNV ATEGRKRHAE
AAAADALTRP AKAAHADTAA AAAAAATNAA ASSYYGHASA SGAAAAAAAA AYQGYYGAYP
SYPAAAYPGQ YPEPMTTKQK KDLLQQKSPA EFFSENKNIA GFDNPGKCLY TTIRELVENA
LDSAESIAVL PLIEITVEEV SKSRLDRIRG VERHDRLDAE LYNDFESEQQ KKRRQEKEAK
DQDKLQKLVN KKGDNAAEVH AKKKEMDAAK KVTQRGNLFY KVTVKDNGSG MPHKDIPNML
GKVLSGTKYG VKQTRGKFGL GAKMALIWSK MTTGLPFEIY SAQKGMSNKS HFILDIDIHR
NEPNVHKEEH QPNAEHWHGA QLSVTIEGNW STYRAKIIKY LRQIAVITPY TEFSFFYKAE
EEKNNVRLVF RRRTDVMPPA PKATKHHPAS VDLELVKRLL LSTTSTNMVQ FLRKELTCIN
ADYAERLVDE MRAGVDITTS PKELNEKQIV RLHQLLHEAR FDEPPGDHLS PAGEYNLRLG
VMKELKPDLI ATHQGDIRTF EGHAFMVEAA VSLGGRDVKP GINVHRFANR IPLLFEGGSD
VITKTALKRI NWSTYKINQN TDKVGVFVSI VSTKIPFKGA GKEYIGDDIE EMVVAVKHAI
QACGVQLKTK IAKALAAREQ KQRKRNLQKY IPDCCNAIWT VLEEMSRVGP HGPKRWKIEE
TTDLLLRVKE KKVSLHTFQA KLTEHIDKID MDMALEYQVQ QGVTTGAVKD EVMLMPRTAF
KHQYGDELHS NVAVLKLLQE F
//
