ID A0A3B6NSN5_WHEAT Unreviewed; 1483 AA.
AC A0A3B6NSN5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=CFC21_084086 {ECO:0000313|EMBL:KAF7079925.1};
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:TraesCS6A02G268600.1};
RN [1] {ECO:0000313|EMBL:KAF7079925.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7079925.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS6A02G268600.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS6A02G268600.1};
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 [3] {ECO:0000313|EnsemblPlants:TraesCS6A02G268600.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7079925.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7079925.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CM022226; KAF7079925.1; -; Genomic_DNA.
DR SMR; A0A3B6NSN5; -.
DR STRING; 4565.A0A3B6NSN5; -.
DR EnsemblPlants; TraesCS6A02G268600.1; TraesCS6A02G268600.1; TraesCS6A02G268600.
DR Gramene; TraesCAD_scaffold_045400_01G000100.1; TraesCAD_scaffold_045400_01G000100.1; TraesCAD_scaffold_045400_01G000100.
DR Gramene; TraesCLE_scaffold_104033_01G000100.1; TraesCLE_scaffold_104033_01G000100.1; TraesCLE_scaffold_104033_01G000100.
DR Gramene; TraesCS6A02G268600.1; TraesCS6A02G268600.1; TraesCS6A02G268600.
DR Gramene; TraesCS6A03G0719400.1; TraesCS6A03G0719400.1.CDS; TraesCS6A03G0719400.
DR Gramene; TraesPAR_scaffold_082236_01G000100.1; TraesPAR_scaffold_082236_01G000100.1; TraesPAR_scaffold_082236_01G000100.
DR Gramene; TraesROB_scaffold_071295_01G000100.1; TraesROB_scaffold_071295_01G000100.1; TraesROB_scaffold_071295_01G000100.
DR Gramene; TraesWEE_scaffold_122517_01G000100.1; TraesWEE_scaffold_122517_01G000100.1; TraesWEE_scaffold_122517_01G000100.
DR OMA; DAAISLX; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000019116; Chromosome 6A.
DR Proteomes; UP000815260; Chromosome 6A.
DR GO; GO:0005634; C:nucleus; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0000819; P:sister chromatid segregation; IBA:GO_Central.
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|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|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 937..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1483
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1483 AA; 166314 MW; 0D927C02D5E7BFE8 CRC64;
MAPAAKKPPL KSSSSHNSAA GDAAGKTIEE MYQKKTQLEH ILLRPDTYVG SVQNHTQTLW
VYEDGAMVNR PVSYVPGLYK IFDEILVNAA DNKQRDPSMD SLKVDIDVEG CCISIYNNGD
GVPVEIHQEE GVYVPELIFG HLLTSSNYDD NERKTTGGRN GYGAKLANIF STEFVIETAD
GHRLKRYRQV FSENMGKKSE PEIKKCKQSE NWTRVTFKPD LAKFNMTELE ADVVALMRKR
VVDMAGTLGK TVKVELNGEK VAVKSFSDYV QLYINSASKE GIDLPRIYQK INDRWEVCVS
LSEGQFQQVS FVNGIATIRG GTHVDYVANQ VASHVMGVVN KKNKQANMKL HTVKGYLWVF
VNALIDNPAF DSQTKETLTT RQGSFGSTCE LSDEFLKKVS SSGVVTNLLS WAEFKLNKEL
KKTDGTKKTS IVGIPKLEDA NDAGGKNSDK CTLILTEGDS AKALAMAGIG VVGRDHYGVF
PLRGKLLNVR EASHKQLMEN AEIQNIKKIL GLQHEKKYDS TKGLRYGHLM IMTDQDHDGS
HIKGLLINFI HKEWPSLLKV PSFLVEFITP IIKATKGKAV KPFYSMPDYE AWKEDLGASA
SSWTIKYYKG LGTSTAEEGR DYFDHIDLHK KDFVWANDEK DNEAIELAFS KKKIAERKEW
LTNYQPGTCL DQREKRIKYS DFINKELILF SMADLERSIP SMVDGFKPGQ RKILFCSFKK
NLTKESKVAQ FIGYVSEHSA YHHGEQSLAS TIIGMAQDFV GSNNINLLEP RGQFGTRNSG
GKDAASARYI FTKLHPITRL IFPKDDDVLL NYLNEDGQSI EPSWYMPIIP MVLVNGSEGI
GTGWSTYVPN YNPRDIIANL KRLLNGETIV PMIPWYRGFK GSLIETSSKA TGVTYTITGV
IEEVADTKLK ITELPVRRWT TDYKEFLESM CPIPIKEKEK SKDKNKEKKK DKDKEKEKSK
EPPLLEEIRS QCDHADVEFE LILTEQNMNI AKQEGLEKKF KLTTTIGTTN MHLFDSHGKI
KKYDTPEDVL KEFFDLRFEF YVKRKKVMLE NMGNELLKYQ NKVRFILAVI SVEIIVNNRK
RADLFDELKQ KGYKAFPKKK PTSGPVAVGS TEADEDNDES PAEAAASDYE YLLAMSIGTL
TMEKVKELIA QQDKVKADLE ILRNTEPNTL WLRDLDALEK ELDVLDAKLE AEQNDRSRKR
AKNSEKAKDS RPAPKKQPKK ATAKSQKAGS DDDVDYKGDI PKPAAQKKKP PPKKASAPVK
DEVKDEEDEV AELKDRLAAY NIDSDNSPEP SAMETEEQQK GKKGRNGPSK RGAAKKAMSS
LAEISDEDIA EPDRESDDGG SSMEVEKKTK GRKPAAEKPK TTIRKRAPAQ TKGMRQKVME
EIFKPTDDST LSAPSPEKKV RRIRDSPFNK KSGSVLHRMA SASTGTEDGE APPSGSSAEP
VAPRRTTRER KAAVVYVASE SEDDETEDED VSEPSDDDFS EDD
//