TOP2_BOMMO
ID TOP2_BOMMO Reviewed; 1547 AA.
AC O16140;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=DNA topoisomerase 2;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE AltName: Full=DNA topoisomerase II;
DE Short=TOPOII;
GN Name=TOP2;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Larsen J.J.;
RT "Cloning of topoisomerase II from the silkworm Bombyx mori.";
RL Submitted (JUL-1997) 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.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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; AF013277; AAB67168.1; -; mRNA.
DR RefSeq; NP_001037009.1; NM_001043544.1.
DR AlphaFoldDB; O16140; -.
DR SMR; O16140; -.
DR STRING; 7091.BGIBMGA011615-TA; -.
DR PRIDE; O16140; -.
DR GeneID; 692558; -.
DR KEGG; bmor:692558; -.
DR CTD; 35225; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_1_0_1; -.
DR InParanoid; O16140; -.
DR OrthoDB; 117851at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; cd00187; TOP4c; 1.
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; Nucleus; Reference proteome; Topoisomerase.
FT CHAIN 1..1547
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145373"
FT DOMAIN 463..580
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 8..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..353
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 996..1005
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1107..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1459..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1459..1516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 813
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 156..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 385..387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 469
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 549
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 549
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 551
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 497
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 500
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 669
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 670
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 731
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 765
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 771
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 812
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 864
FT /note="Important for DNA bending; intercalates between base
FT pairs of target DNA"
FT /evidence="ECO:0000250"
FT SITE 938
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
SQ SEQUENCE 1547 AA; 176184 MW; EDFE086253F22CEE CRC64;
MADIKSMFNK MSSPKQNGTG EPAPAKGQKG AIEKIYQKKS QLEHILLRPD TYIGSVERAT
ETMWVYDKVK ECMMQKELTS VPDCSFPGLY KIYDEILVNA ADNKQRDPKM DVIKIDINQE
TNTISVYNNG SGIPVVMHKD EKMYVPTMIF GHLLTSSNYN DEEEKVTGGR NGYGAKLCNI
FSTKFTVETA SKQYKKHFKQ TWGSNMTKAS EPKIKDSGKD DDFTKIVFSP DLAKFKMEKL
EDDIVLLMSR RAYDVAASSQ GVKVYLNGER LKINKFKDYV DLYIKGKDDE NGQPLKVVYE
KVSDRWEVAL TISDMGFQQV SFVNSIATTK GGKHVDTVAD SVVKNVLEVL KKKNKGGVNI
KPYQVKTHMW LFVNCLIVNP TFDSQTKENM TLQAKSFGSK CNLSEKFITA VTKCGLVESV
LTWAKFKAQD QLVKASGKKQ SKLKGIPKLE DANDAGTKNA HLCTLILTEG DSAKTLAVSG
LSVVGRDHYG VFPLEGKPLN VRDASHKQVL ENVEINNLIK ILGLQYKKKY NSVDDLKTLR
YGKVMIMADQ DQDGSHIKGL IINFIHHNWP ELLKLPFLEE FITPIVKATK KDKEISFYSL
PEFEEWKKET ENHHTYNIKY YKGLGTSTSK EAKEYFQNMD RHRIRFKYSG PTDDHHIELA
FSKKGADQRK EWLTNHMDEV KRRKEIGLSE RYLYTKETKT VTYSDFVNLE LVLFSNGDNV
RSIPSMIDGL KPGQRKVIFT CIKRNDKREV KVAQLAGSVA EHSAYHHGEQ SLAMTIVNLA
QNYVGSNNIN LLEPRGQFGT RLSGGKDSAS PRYIFTLMSP LTRLIFHPHD DPLLVHEFED
NQKIEPVYYL PIIPMVLVNG VEGIGTGWST KIPNYNPRDI AENLRRLLDG EKPKVMHPWY
KNFKGNVEGF GDKYVISGEA AILPGDKIEI TELPVGTWTH NYKENVLEPM LGTDKVKPLI
SEYREYNTDT TVRFVVSLLP GKLSEIEAEG IHKVFKLQTT ISMTCMNAFD YNCCLEKYDK
VEEILREFYD LRVKYYVRRK DYLEGQLQAE ADKLSNQARF ILKKCDKGLV IENKKRKAMV
EELIKRGYAP DPIADWKKRA SKIQGLTALE DDDAQESEEE EPEPDPKGKP VDPDKAFQQL
KEVKKFNYLL GMSMWMLTKE KKDELLKQRD QKLTELTTLK NKTAPMLWRE DLDAFLIKLD
EVEDKERREE LNVNKKTSKA MAGKKNRKSM FDIIPSENGR RVEPKISDDL IKRIQAAEKA
KTRKEIKKEY DPDDPTGISP SSGEKKPKAR VKKEKPEKAE KPDKVDKAEK TDGLKQTKLT
FKKEPKKKKM TFSGSSSGEM SASDAEVEVL VPRERTNARR AATRVQKYKD GSDDSGSDSE
PELLDNKIDS DHEAPQTLSI SDEDDDFNIK KNPAKKPAEM DSDCLFDSLI EDAKKDEPQK
TLTKSKSESI LIRRLNIERQ RRCDTSVPPK EKAAPKRKLM NVDKDEKKTK KRPARVMLDQ
DSDDEDSIFD SKKGKKKTAA NPKKKAKKKV ESDSESDFNI SDSSLSD
