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Database: UniProt
Entry: A0A3B6NSN5_WHEAT
LinkDB: A0A3B6NSN5_WHEAT
Original site: A0A3B6NSN5_WHEAT 
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
//
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