ID A0A3B6PQK3_WHEAT Unreviewed; 1458 AA.
AC A0A3B6PQK3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS6B02G295700.1};
RN [1] {ECO:0000313|EnsemblPlants:TraesCS6B02G295700.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS6B02G295700.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS6B02G295700.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
CC -!- FUNCTION: Control of topological states of DNA by transient breakage
CC and subsequent rejoining of DNA strands. Topoisomerase II makes double-
CC strand breaks. {ECO:0000256|RuleBase:RU362094}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185,
CC ECO:0000256|RuleBase:RU362094};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080, ECO:0000256|RuleBase:RU362094}.
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DR EnsemblPlants; TraesCS6B02G295700.1; TraesCS6B02G295700.1; TraesCS6B02G295700.
DR Gramene; TraesCS6B02G295700.1; TraesCS6B02G295700.1; TraesCS6B02G295700.
DR Gramene; TraesCS6B03G0851600.1; TraesCS6B03G0851600.1.CDS; TraesCS6B03G0851600.
DR OMA; ERWILIM; -.
DR Proteomes; UP000019116; Chromosome 6B.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd16930; HATPase_TopII-like; 1.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.1490.30; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR InterPro; IPR003594; HATPase_C.
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; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR001154; TopoII_euk.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034157; TOPRIM_TopoII.
DR PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR PRINTS; PR01158; TOPISMRASEII.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 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; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362094};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362094};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362094};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362094};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 451..565
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1458
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1458 AA; 163587 MW; 7C35A40D9B1CBF2A CRC64;
MPPAAKKPPL KSSSSHNSAA GDAAGKTIEE MYQKKTQLEH ILLRPDTYVG SIEKHTATLW
VYEDGAMVNR PVTYVPGLYK IFDEILVNAA DNKQRDPSMD SLKVDIDVEG CCISIYNNGD
GVPVEIHQEE KIYVPELIFG NLLTSSNYDD NERKTTGGRN GYGAKLANIF STEFVIETAD
GRRQKRYKQV FSENMGKKSE PEIKKCKQSE NWTKVTFKPD LEKFKMTELE ADVVALMMKR
VVDMAGTLGK TVKVELNGEK VAVKSFSDYV QLYIDSASKE GIKLPRIYQK VNDRWEVCVS
LSEGQFQQVS FVNGIATIKG GTHVDYVASQ IASHVMGVVN KKNKQANMKL HIVKGYLWVF
VNALIDNPAF DSQTKETLTT RQGSFGSTCE LPEDFLKKVS SSGVVDSLLS WAEFKLSKEL
KKTDGTKKTS IVGIPKLEDA NDAGGKNSDQ CTLILTEGDS AKALAMAGIG VVGRDHYGVF
PLRGKLLNVR EASHKQLMEN AEIQNIKKIL GLQHEKKYDS TKGLRYGHLM IMTDQDHDGS
HIKGLLINFI HKEWPSLLKV PSFLVEFITP IIKATKGKTV RPFYSMPDYE AWKESLGASA
SSWTIKYYKG LGTSTAEEGR DYFEQISLHK KDFVWADDKD GEAIELAFSK KKITERKDWL
TNYQPGTCLD QREKRIKYSD FINKELILFS MADLERSIPS MVDGFKPGQR KILFCSFKKN
LVKESKVAQF IGYVSEHSAY HHGEQSLAST IVGMAQDFVG SNNINLLEPR GQFGTRNAGG
KDAASARYIF TRLNPITRLI FPKDDDVLLN YLNEDGQSIE PSWYMPIIPM VLVNGSEGIG
TGWSTYVPNY NPRDIIANLK RLLNGETIVP MVPWYRGFKG SLKETSTKAT GVTYTITGVI
EEVADTKLKI TELPVRRWTT DYKEFLESMC PIPIKEKEKS KDKNKEKKKE KDKDKDKEKE
KSKEPPLLEE IRSQCDHADV EFELILTEQN MNIAKQEGLE KKFKLTTTIG TTNMHLFDSH
GKIKKYDNPE DVLQEFFDLR FKFYIKRKKV MLENMGQELL KYQNKVRFIL AVTSGEIIVN
NRKRADLFQE LQKKNYTPFP KKKPTSGPVA VGSTEADEDN DESPAEAAAS DYEYLLAMSI
GTLTMEKVKE LIAQQNKVLD AKLEAEQNDR SRKRAKNSEK ARDPKPATKK QPKKATAKSQ
KAGSDDDVDY KGDILKPAAQ KKKPPPKKAS APVKDEVKDE EDEVAELKDR LAAYNIHSDN
SPEPSAMETE EHQEGKKGRN GPSKRGAAKK AMSSLAEISD EDIAEPHHES EDGGSSMEVE
KKTKGRKPAA EKPKTTIRKR APTQSKGMRQ KVMEEIFKPT DDSTLSAPSP EKKVRRIRDS
PFNKKSGSVL HRMASSSTGT EDAEAPPSGS SAETVVPRRT TRERKAAVVY VASESEDDES
EDEDVSEPSD DDDFSEDD
//
