ID A0A3B6QGT5_WHEAT Unreviewed; 1606 AA.
AC A0A3B6QGT5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=CFC21_093275 {ECO:0000313|EMBL:KAF7090544.1};
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:TraesCS6D02G246300.1};
RN [1] {ECO:0000313|EMBL:KAF7090544.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7090544.1};
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:TraesCS6D02G246300.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS6D02G246300.1};
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:TraesCS6D02G246300.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7090544.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7090544.1};
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; CM022228; KAF7090544.1; -; Genomic_DNA.
DR SMR; A0A3B6QGT5; -.
DR STRING; 4565.A0A3B6QGT5; -.
DR PaxDb; 4565-Traes_6DL_2BA26E6A2-2; -.
DR EnsemblPlants; TraesCS6D02G246300.1; TraesCS6D02G246300.1; TraesCS6D02G246300.
DR Gramene; TraesCAD_scaffold_131275_01G000100.1; TraesCAD_scaffold_131275_01G000100.1; TraesCAD_scaffold_131275_01G000100.
DR Gramene; TraesCLE_scaffold_123374_01G000100.1; TraesCLE_scaffold_123374_01G000100.1; TraesCLE_scaffold_123374_01G000100.
DR Gramene; TraesCS6D02G246300.1; TraesCS6D02G246300.1; TraesCS6D02G246300.
DR Gramene; TraesCS6D03G0602900.2; TraesCS6D03G0602900.2.CDS; TraesCS6D03G0602900.
DR Gramene; TraesPAR_scaffold_038327_01G000100.1; TraesPAR_scaffold_038327_01G000100.1; TraesPAR_scaffold_038327_01G000100.
DR Gramene; TraesROB_scaffold_045593_01G000100.1; TraesROB_scaffold_045593_01G000100.1; TraesROB_scaffold_045593_01G000100.
DR Gramene; TraesWEE_scaffold_040494_01G000100.1; TraesWEE_scaffold_040494_01G000100.1; TraesWEE_scaffold_040494_01G000100.
DR OMA; QEMGYDS; -.
DR Proteomes; UP000019116; Chromosome 6D.
DR Proteomes; UP000815260; Chromosome 6D.
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|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 569..683
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1055..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1217..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1457..1486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1537..1553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1606
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1606 AA; 179964 MW; 0918AA347347D565 CRC64;
MHPLLPCFFP ETTLFSRVKP SKGTERLEYV GTHTLPCAFT PVAVSRIPHP TGRTRWAHTR
NVARSPNSNF ESPRSPLPVH FKPHPIPLPL PQIPNSKPHP AFPPTPQTLA RTQPLCAAMA
PAAKKPPLKS SSSHNSAAGD AAGKTIEEMY QKKTQLEHIL LRPDTYVGSV QNHTQTLWVY
EDGAMVNRPV SYVPGLYKIF DEILVNAADN KQRDPSMDSL KVDIDVEGCC ISIYNNGDGV
PVEIHQEEGV YVPELIFGHL LTSSNYDDNE RKTTGGRNGY GAKLANIFST EFVIETADGH
RLKRYRQVFS ENMGKKSEPE IKKCKQSENW TRVTFKPDLA KFNMTELEAD VVALMRKRVV
DMAGTLGKTV KVELNGEKVA VKSFSDYVQL YINSASKEGI DLPRIYQKIN DRWEVCVSLS
EGQFQQVSFV NGIATIRGGT HVDYVANQVA SHVMGVVNKK NKQANMKLHT VKGYLWVFVN
ALIDNPAFDS QTKETLTTRQ ASFGSTCELS DEFLKKVSSS GVVTNLLSWA EFKLSKELKK
TDGTKKTSIV GIPKLEDAND AGGKNSDKCT LILTEGDSAK ALAMAGIGVV GRDHYGVFPL
RGKLLNVREA SHKQLMENAE IQNIKKILGL QHEKKYDSTK GLRYGHLMIM TDQDHDGSHI
KGLLINFIHK EWPSLLKVPS FLVEFITPII KATKGKSVKP FYSMPDYEAW KEDLGASASS
WTIKYYKGLG TSTAEEGRDY FEHIALHKKD FVWADDKEDG EAIELAFSKK KISERKDWLT
NYQPGTCLDQ REKRIKYSDF INKELILFSM ADLERSIPSM VDGFKPGQRK ILFCSFKKNL
LKESKVAQFI GYVSEHSAYH HGEQSLASTI IGMAQDFVGS NNINLLEPRG QFGTRNAGGK
DAASARYIFT RLQPVTRLIF PKDDDVLLNY LNEDGQSIEP SWYMPIIPMV LVNGSEGIGT
GWSTYVPNYN PKDIIANLKR LLNGETIVPM VPWYRGFKGS LKETSSKATG VTYTITGVIE
EVADTKLKIT ELPVRRWTTD YKEFLESMCP IPIKEKEKSK DKNKEKKKDK DKDKDKEKEK
SKEPPLLEEI RSQCDHADVE FELILTEQNM NIAKQEGLEK KFKLTTTIGT TNMHLFDSHG
KIKKYDTPED VLQEFFDLRF EFYVKRKKVM LENMGNELLK YQNKVRFILA VISGKIIVNN
RKRADLFQEL KQQGYKPFPK KKPTSGPVAV GSTEADEDND ESPAEAAASD YEYLLAMSIG
TLTMEKVKEL IAQQDKVEAD LEILRNTEPK TLWLRDLDAL EKELDVLDAK LEAEQNDRSR
KRAKNSEKAK DPKPATKKQP KKATAKSQKA GSDDDVDYKG DILKPAAQKK KPPPKKASAP
VKDEVKDEED EVAELKDRLA AYNIDSDNSP EPSAMETEEQ QKGKKGWNGP SKRGAAKKAM
SSLAEISDED VAEPDHESDD GGSSMEVEKK TKGRKPAAEK PKTTIRKRAP AQTKGMRQKV
MEEIFKPTDD STLSAPSPEK KVRRIRDSPF NKKSGSVLHR MASSSTGTED AEAPPSGSSA
EPVVPRRTTR ERKAAVVYVA SESEDDESED EDVSEPSDDD DFSEDD
//
