TOP2_MIMIV
ID TOP2_MIMIV Reviewed; 1263 AA.
AC Q5UQE6;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=DNA topoisomerase 2;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE AltName: Full=DNA topoisomerase II;
GN Name=TOP2; OrderedLocusNames=MIMI_R480;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
CC -!- FUNCTION: Can introduce negative superhelical turns into double-
CC stranded circular DNA.
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 -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
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DR EMBL; AY653733; AAV50746.1; -; Genomic_DNA.
DR RefSeq; YP_003986988.1; NC_014649.1.
DR SMR; Q5UQE6; -.
DR PRIDE; Q5UQE6; -.
DR GeneID; 9925106; -.
DR KEGG; vg:9925106; -.
DR Proteomes; UP000001134; Genome.
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; -; 2.
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; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 2.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF56719; SSF56719; 2.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..1263
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145390"
FT DOMAIN 439..553
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 329..331
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 977..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1077
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 1244..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 828
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 137..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 150..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 362..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 445
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 522
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 522
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 524
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 473
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 476
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT SITE 695
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT SITE 696
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT SITE 745
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT SITE 780
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT SITE 786
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT SITE 827
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 954
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
SQ SEQUENCE 1263 AA; 143449 MW; 411533D3BB51B502 CRC64;
MSKTSKSNKN PKSIEEKYQK KNLHEHILHS PDTYIGSIEE KTCNMWIFNE SAGEDDAKII
FKEITYVPGL YKIYDEVIVN AADHNKRCQT CNIIKVDIDQ KTGQISVWNN GDGIDVAIHK
EHNIWVPSMI FGELLTSTNY DKNEEKTVGG KNGFGAKLAN IYSVEFTIET VDANKGKKFF
QRFTNNMYDK EEPKISSFKK SSYTKITFIP DFKKFGLKCL DDDTLALFKK RVFDLAMTTN
AKVYFNDKQI VQNNFKKYVG LYFPEGSQHK VVIDDTTHER WKVGVIYDPT DQLEHQNISF
VNSICTSRGG THVEQVVGQI VNGLKTAIVK KAKNVQIKPA MIKENLIFFV DATIVNPDFD
TQTKEYLTKK AANFGSKFEV TEKFIKGVIK TGVCDQIIAN AKAREEANLS KTDGKGRGPV
RYEKLYNAHK AGTKEGYKCT LILTEGDSAK TFAMSGLNVI GRDYYGVFPL RGKLLNVRDA
SPKKIADNEE ITAIKKIVGL EQGKVYDDLK GLRYGSIMIL ADQDVDGYHI KGLIMNFIHC
FWPSLVKYEG FIQSFATPLL KATKGKGKTK QVVAFTSPQS FEEWKKENND GKGWSIKYYK
GLGTSDPAEA QECFADLNDK LVKYFWEPKK KNLESESNSK SVDSNKSKTT NKKKIESEFI
EEESDIISDT YKPKNKDISE DAMTLAFAGG REDDRKIWIN TYNPDNYLDP SKKRISYYDF
IHKELITFSV DDVLRSVPNL MDGFKPSHRK VFYGSVEKNI YKQEIKVSDL TGFVSNMTKY
HHGDQSLSST IVGMAQNYVG SNNLNLLMPL GMFGSRLTGG KDSASPRYLN TKLDDLAKKI
FIDYDFDILQ HQSEDNCRIE PVYYAPIIPM ILVNGAEGIG TGYSTKIYPC NPRDIIANIK
RLLTNENPKT MKPWFRHLTG TIEKIDGAKY ISRAKYEIIG KDTIHITDLP VGIWTDNYKA
FLDNLIVQGT AQNAEEKKAS KAVSSAKNTK TTTKAGSKTG SRTRKNPALA KKSQKSVTAK
VAKKNPVASS IKTYSEDCTD IRISFTIVFH PGKLDTLIKS GKLDTGLKLV KPLNLTNMHL
FNEKGKIKKY DTYGAILRNF VKVRLNLYQK RKDYLLGKWK KEMDILKWKV KFIEYVIEGK
IVIFKNGKSK KKEEVLKALE DLKFPKFIVG NESYPSYGYI TSIGLFNLTL EEVEKLKKQL
ADKKQELAIL EAKSPEEIWE EELDEFVEAY DIWEKEVDEN YNDLLNKKKG STGKKSRKTS
TQK
