ID A0A0D9Y5Q2_9ORYZ Unreviewed; 380 AA.
AC A0A0D9Y5Q2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, 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};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM01G09680.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM01G09680.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM01G09680.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0D9Y5Q2; -.
DR STRING; 40148.A0A0D9Y5Q2; -.
DR EnsemblPlants; OGLUM01G09680.1; OGLUM01G09680.1; OGLUM01G09680.
DR EnsemblPlants; OGLUM01G09680.2; OGLUM01G09680.2; OGLUM01G09680.
DR Gramene; OGLUM01G09680.1; OGLUM01G09680.1; OGLUM01G09680.
DR Gramene; OGLUM01G09680.2; OGLUM01G09680.2; OGLUM01G09680.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_0_2_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
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 Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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 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:UP000026961};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 276..341
FT /note="DNA topoisomerase type IIA subunit B"
FT /evidence="ECO:0000259|Pfam:PF00204"
SQ SEQUENCE 380 AA; 42726 MW; 4BD9F6BFD112990F CRC64;
MATSNRYFLL RSCLNGHSAA GVRHESPAAA ARCGGGGGDT TLRERILLRP DGYIGSPEKR
TQTFWINDGY YMVPREVTYR PGLHRIFDEV LVHAASSKRR DPAMDALSVE VDVVERSVSV
FFNGRGGAAP VELVDEEERG VYAPEVFFGH LHDDDVEVDR NKTTNGGGGG YGFVVEIADG
CRMKKYKQVF SENMGKKSVP HITDCNQGEN WTMITFKPDL ARFNMTYLEE DHVTLMWKRV
VDMAGILGDS VRVEWDGVRL LINSFDDYVR LHIDSPTLKG GTHVDYVTEL ITNHLMNLLN
EHYEECNFNV DDVKRYLWVF LNVIIDNPTF DSQTKETLTT PPGRFGSKLE LPDTFGNGLI
RRLFGYRGPL DAKAGVSSRD
//
