ID A0A251VP40_HELAN Unreviewed; 1499 AA.
AC A0A251VP40;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN Name=TOPII {ECO:0000313|EMBL:OTG37224.1};
GN ORFNames=HannXRQ_Chr01g0016471 {ECO:0000313|EMBL:OTG37224.1},
GN HanXRQr2_Chr01g0025721 {ECO:0000313|EMBL:KAF5822370.1};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG37224.1, ECO:0000313|Proteomes:UP000215914};
RN [1] {ECO:0000313|EMBL:KAF5822370.1, ECO:0000313|Proteomes:UP000215914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5822370.1};
RX PubMed=28538728; DOI=10.1038/nature22380;
RA Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA Vincourt P., Rieseberg L.H., Langlade N.B.;
RT "The sunflower genome provides insights into oil metabolism, flowering and
RT Asterid evolution.";
RL Nature 546:148-152(2017).
RN [2] {ECO:0000313|EMBL:OTG37224.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaves {ECO:0000313|EMBL:OTG37224.1};
RA Langlade N., Munos S.;
RT "Sunflower complete genome.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF5822370.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:KAF5822370.1};
RA Gouzy J., Langlade N., Munos S.;
RT "Helianthus annuus Genome sequencing and assembly Release 2.";
RL Submitted (JUN-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; MNCJ02000316; KAF5822370.1; -; Genomic_DNA.
DR EMBL; CM007890; OTG37224.1; -; Genomic_DNA.
DR STRING; 4232.A0A251VP40; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr01g0025721; mRNA:HanXRQr2_Chr01g0025721; HanXRQr2_Chr01g0025721.
DR Gramene; mRNA:HanXRQr2_Chr01g0025721; mRNA:HanXRQr2_Chr01g0025721; HanXRQr2_Chr01g0025721.
DR InParanoid; A0A251VP40; -.
DR OMA; TWTQDFK; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000215914; Chromosome 1.
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:UP000215914};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 449..563
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1302..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1499
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1499 AA; 168683 MW; BF818D5483333CC1 CRC64;
MATDHREPLH STTTDNIPPT TKPTKKAART IEETYQKKTQ LEHILLRPDT YIGSIEKHEQ
TLWVWENDQM VKRPISYVPG LYKIFDEILV NAADNKQRDP KMDSVKVNID VGNNLISVYN
NGDGIPVEIH QEEKVYVPEL IFGHLLTSSN YDDSIKKTTG GRNGYGAKLA NIFSTEFTIE
TADGKRNRRY KQVFTNNMGK KLEPTITKCK NSENWTMVSF KPDLSKFGME CLEDDVVALM
KKRVVDLAGC LGKSVKVELD GKRVPPKTFE DYVKLYLQPS TDTLRIYEKV NERWEICVSI
ADGHFEQVSF VNNIATIKGG THVDYITNQI ANHLVTVVKK QNKHANLKAH NVKNYLWVFV
NALIDNPAFD SQTKETLTIK QSSFGSTCEL SPEFLKKVAK SDIVKRVVSW VQFKQQNDLK
KTDGNKRGKL NIPKLEEANF AATNNSDNCT LILTEGDSAK ALAMSGLSVV GQDYYGVFPL
RGKLLNVREA SPKQLQENAE IQNIKKILGL QHGKIYDNVK SLRYGHLMIM ADQDHDGSHI
KGLLINFLHS FWPSLLKVPE FVLEFITPIV KATNKKTKNV ISFYTMPEYE AWKENLGHKA
REYKIKYYKG LGTSNGKEGA EYFADLEKHK KDFVWADDED GDAIELAFSK KKIEARKNWL
RALQAGTFFD SKEKHIPYRD FINKELILFS MADLQRSIPS MVDGLKPGQR KILFCAFKKP
IFQEVKVAQF SGYVSEHSAY HHGEQSLVST IIGMAQNFIG SNNINLFYPS GQFGTRQMGG
KDHASGRYIY TKLSPITRHL FHKADELLLN YLNEDGQSIE PTWFIPIIPM VLVNGSEGIG
TGWSSFIPNY NPRDIIANLK RLLNGEQMVP MDPWYKWFKG TIQKTTSKDT GYTTVGVFEE
NEDNNSLNIT ELPIRRWTQE YKEFLEAASL SGKDKEPFIE EYNAHNDDTT VHFEVVMTAN
QMNKAKEEGL LKKFKLTTTL STSNMHLFDA NGVIKKYDTP EQILEDFFHL RLDYYEKRKN
ALLHELGKAS LQLENKVRFI REVVEGTLVV SNRKKADLCA ELKVKGYTPL PKEAVLEASI
AGAVDHVEGS EETEEGSEEE TAEMAVEEQK PSAGTASKTI PGTEYDYLLS MAIGTLTYEK
MQQLWHERDT KKAEFDELTN TPSKSLWLRD LDSLNNQLDE QDKRDAKDEA ERRKQQEKAR
AKGPGGGRNA RKPARKAVTK KPSATSAVVI EPMDTSANDV PVPKPRGKAA GQKKAPAKGK
GKATLVDEDD DEIPSLAERM AQQNLHSVQD GEIVELEDRL AKHNIESSPD QEEVPKKKAP
AKRPAAAKKK ATTIISDDEN EEDIDLSDDS DFEVLVAPPE EKKKGGRKPA AAKPPAAAAT
KKRGAAAGAA AKTSKQTGGQ KLITEVLKPV VEASPEKKVR KMRPSPFNKK SGSVLNKKGE
EEKEEDEMVV GESSGEVGAK ARPQRANRKK MTYVISDSEE EDEEVDDEAS EDSDFDDDE
//
