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Database: UniProt
Entry: A0A3B6REZ8_WHEAT
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ID   A0A3B6REZ8_WHEAT        Unreviewed;       387 AA.
AC   A0A3B6REZ8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE            EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN   ORFNames=CFC21_096574 {ECO:0000313|EMBL:KAF7094248.1};
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:TraesCS7A02G157900.1.cds1};
RN   [1] {ECO:0000313|EMBL:KAF7094248.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7094248.1};
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:TraesCS7A02G157900.1.cds1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS7A02G157900.1.cds1};
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:TraesCS7A02G157900.1.cds1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KAF7094248.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7094248.1};
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   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC       {ECO:0000256|RuleBase:RU362094}.
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DR   EMBL; CM022229; KAF7094248.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B6REZ8; -.
DR   SMR; A0A3B6REZ8; -.
DR   STRING; 4565.A0A3B6REZ8; -.
DR   EnsemblPlants; TraesCS7A02G157900.1; TraesCS7A02G157900.1.cds1; TraesCS7A02G157900.
DR   Gramene; TraesCLE_scaffold_038610_01G000100.1; TraesCLE_scaffold_038610_01G000100.1; TraesCLE_scaffold_038610_01G000100.
DR   Gramene; TraesCS7A02G157900.1; TraesCS7A02G157900.1.cds1; TraesCS7A02G157900.
DR   Gramene; TraesCS7A03G0369500.1; TraesCS7A03G0369500.1.CDS1; TraesCS7A03G0369500.
DR   Gramene; TraesKAR7A01G0078710.1; cds.TraesKAR7A01G0078710.1; TraesKAR7A01G0078710.
DR   Gramene; TraesRN7A0100340800.1; TraesRN7A0100340800.1; TraesRN7A0100340800.
DR   Gramene; TraesROB_scaffold_026480_01G000200.1; TraesROB_scaffold_026480_01G000200.1; TraesROB_scaffold_026480_01G000200.
DR   Gramene; TraesWEE_scaffold_046340_01G000200.1; TraesWEE_scaffold_046340_01G000200.1; TraesWEE_scaffold_046340_01G000200.
DR   OMA; YPRICIV; -.
DR   Proteomes; UP000019116; Chromosome 7A.
DR   Proteomes; UP000815260; Chromosome 7A.
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   CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
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; IPR013506; Topo_IIA_bsu_dom2.
DR   PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1.
DR   PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   PRINTS; PR00418; TPI2FAMILY.
DR   SMART; SM00433; TOP2c; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362094};
KW   DNA-binding {ECO:0000256|RuleBase:RU362094};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362094};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362094};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW   Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT   DOMAIN          218..363
FT                   /note="DNA topoisomerase type IIA subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF00204"
SQ   SEQUENCE   387 AA;  43825 MW;  ADC8C85BDC32C766 CRC64;
     MYKKKNTPLE QILLRPDTHV GSVEKHTQTL WVYKEGAMVH SPVTYVPGLH NIFDEILVQA
     ADNLQRDPSM DSLRVDIDVE RCCISVYNNG NGMPVEIHQE EGLYVPEMMR MSYGAVLANI
     FSTEFVIETA DGRRQKKFKQ VFSENMGKKS EPEITECEPS DNWTRVTFKP DLAKFNMTVL
     EDDAVALMRK RVVDMAGTLG ETVKVELNGE KLSAKSFSDY VQLYIDSASK EGIELPRIYQ
     RVNDRWEVCV SLNEGQFHQV SFVNRIATLR GGTHVDYVAD QIANHVMGVV NKRNKHANMK
     LHTVKGYLWV FVNALIDNPA FDLQTKETLT THQGTFGSKC ELSEDFLNRV SNSGVVNKLL
     SFAEFRLSKG LHKTDGSKRK VLLPSLS
//
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