TOP2_PEA
ID TOP2_PEA Reviewed; 1462 AA.
AC O24308;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=DNA topoisomerase 2;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE AltName: Full=DNA topoisomerase II;
DE AltName: Full=PsTopII;
GN Name=TOP2; Synonyms=TOPII;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=10561074; DOI=10.1023/a:1006352820788;
RA Reddy M.K., Nair S., Tewari K.K., Mudgil Y., Yadav B.S., Sopory S.K.;
RT "Cloning and characterization of a cDNA encoding topoisomerase II in pea
RT and analysis of its expression in relation to cell proliferation.";
RL Plant Mol. Biol. 41:125-137(1999).
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.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00995};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges
CC with both the protein and the DNA. Can also accept other divalent metal
CC cations, such as Mn(2+) or Ca(2+). {ECO:0000255|PROSITE-
CC ProRule:PRU00995};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Abundant in proliferative tissues.
CC -!- INDUCTION: By light and growth factors.
CC -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC negative and positive supercoils, whereas prokaryotic enzymes relax
CC only negative supercoils.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
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DR EMBL; Y14559; CAA74891.1; -; mRNA.
DR PIR; T06819; T06819.
DR AlphaFoldDB; O24308; -.
DR SMR; O24308; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
DR Gene3D; 1.10.268.10; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.90.199.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_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; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034157; TOPRIM_TopoII.
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 SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Topoisomerase.
FT CHAIN 1..1462
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145381"
FT DOMAIN 442..556
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 332..334
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 947..956
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1040..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1300
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1462
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 761
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 136..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 149..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 365..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 448
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 525
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 525
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 527
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 476
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 479
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 648
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 649
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 713
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 719
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 760
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 812
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
FT SITE 888
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
SQ SEQUENCE 1462 AA; 164206 MW; D9212C54AE0F8B2E CRC64;
MEKRPLQTSN AANIPSKTIE EMYQKKTQLE HILLRPDTYV GSIEKHTQNL WVYENDEMVH
RAVSYVPGLY KIFDEILVNA ADNKQRDPSM DSLKVTIDPE ANTVSVYNNG DGVPVEIHQE
EKVYVPELIF GHLLTSSNYD DNVKKTTGGR NGYGAKLTNI FSTEFIIETA DGRRLKKYKQ
VFSNNMGTKC EPVITKCKAS ENWTKVTFKP DLEKFKMAYL EEDVVALMKK RVLDMAGCFG
KTVKVELNGT LIRFKSFRDY ADLFLKCAEK SKPMPLPRIH AKVGDRWEIC ISLSDGQFQQ
VSFVNSIATI KGGTHVDYIT NQITTYIMNK VNKKKKDANV KAHTVKNHLW VFVNSLIDNP
AFDSQTKETL TTRQASFGSK CDVPESMLKD VEKSGIVDTL LSWADFKQSK DLKKTDGTKT
QRLRGCKAED ANEAGGRNSE KCTLILTEGD SAKALAMAGL SVVGRDHYGV FPLRGKLLNV
REASSKQIMD NEEIQNIKKI LGLQQNKEYT NVKSLRYGHL MIMADQDHDG SHIKGLLINF
IHSFWPSLLK VPSFLVEFTT PVIRASHPNK TITSFYSMPE YEAWKERLGN SATSWKIKYY
KGLGTSTPQE GREYFSDLGR HRKDFIWDDE LDGNAIELAF SKKKAEGRKI WMRNFEPGTC
RDHEAKLINY KDFVNKELIL FSRADLFGSF KKKLYKEIKV AQFIGYVSEH SAYHHGEQSL
ASTIIGMAQD FVGSNNINLL KPNGQFGTCN LGGKDHASAR YIYTELSPVT RCLFHEHDDK
LLEYLNEDGK SIEPNWYMPI IPLVLVNGSE GIGTGWSSYI PNYNPREIIA NVRRLLNGEE
LVPMDPWYKG FRGTIEKSAK EGGYIVNGTV TEIDEQTFRI TELPIRKWTQ DYKQFLESIT
DGAPNVKDPL IEDFRQNGDD AIVDIEIKMK PEKIATILQE GLFKKFKLTS TISTSNMHLF
DAEGNKKFDT PEQILEEFFP LRLDYYEKSK EYILGNLNRL LLILDNKVRF ILGVVNGEII
VSNRKKAELL IELKEKGFTP MPRKGKSTKP QVAGANDDDS EEQEDAEPET ASQSVSVEGA
TWGDYDDLLS LPIGTLTLES VQKLLDEKTE KEKEYEILSG TPTTSLWLKD LDEFEKKLDE
LDLKYAEDDR KRASQGSKKA NGFASKPAKK PPQPRKNTKK AKSVEPENDN SSMEIENAVE
AAKPAEVAKP KGRAAPKKNI QKEPEDDIQS LQERLAAYNI ESSGEKSQAM ESEEVQQKAA
GKKQNNKRGG AKKKSSTIVL ESDSDNEVND VDDDDDDFEE VQQKAAPVKK GGRKPAAQNA
KKAPAKAPAK APAAPKKRSV GTKQSAGQKL LTDMLQPAEG TGTSPEKKVR KMRESPFNKK
SGSILGRAAA AKDISPIADC SAGSASNTPL SEDEVVEIAP QPARARPQRA NRTQMKYALS
ESESEEDSDE DAELSDFEED DD
