ID   TOP2_ASFB7              Reviewed;        1192 AA.
AC   Q00942;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=DNA topoisomerase 2 {ECO:0000303|PubMed:25463606};
DE            EC=5.6.2.2 {ECO:0000269|PubMed:25463606};
DE   AltName: Full=DNA topoisomerase II;
GN   Name=TOP; OrderedLocusNames=Ba71V-112; ORFNames=P1192R;
OS   African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10498;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=1316688; DOI=10.1016/0042-6822(92)90558-7;
RA   Garcia-Beato R., Freije J.M.P., Lopez-Otin C., Blasco R., Vinuela E.;
RT   "A gene homologous to topoisomerase II in African swine fever virus.";
RL   Virology 188:938-947(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA   Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA   Rodriguez J.F., Vinuela E.;
RT   "Analysis of the complete nucleotide sequence of African swine fever
RT   virus.";
RL   Virology 208:249-278(1995).
RN   [3]
RP   REVIEW.
RX   PubMed=23041356; DOI=10.1016/j.virusres.2012.09.014;
RA   Rodriguez J.M., Salas M.L.;
RT   "African swine fever virus transcription.";
RL   Virus Res. 173:15-28(2013).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP   TYR-800.
RX   PubMed=25463606; DOI=10.1016/j.virol.2014.10.034;
RA   Coelho J., Martins C., Ferreira F., Leitao A.;
RT   "African swine fever virus ORF P1192R codes for a functional type II DNA
RT   topoisomerase.";
RL   Virology 474:82-93(2015).
RN   [5]
RP   FUNCTION.
RX   PubMed=27060564; DOI=10.1016/j.virol.2016.03.023;
RA   Coelho J., Ferreira F., Martins C., Leitao A.;
RT   "Functional characterization and inhibition of the type II DNA
RT   topoisomerase coded by African swine fever virus.";
RL   Virology 493:209-216(2016).
RN   [6]
RP   FUNCTION.
RX   PubMed=28381576; DOI=10.1128/jvi.02498-16;
RA   Frouco G., Freitas F.B., Coelho J., Leitao A., Martins C., Ferreira F.;
RT   "DNA-Binding properties of African swine fever virus pA104R, a histone-Like
RT   protein involved in viral replication and transcription.";
RL   J. Virol. 91:0-0(2017).
RN   [7]
RP   INDUCTION.
RX   PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA   Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA   Dixon L., Werner F.;
RT   "The African Swine Fever Virus Transcriptome.";
RL   J. Virol. 94:0-0(2020).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=33429879; DOI=10.3390/v13010077;
RA   Aicher S.M., Monaghan P., Netherton C.L., Hawes P.C.;
RT   "Unpicking the Secrets of African Swine Fever Viral Replication Sites.";
RL   Viruses 13:0-0(2021).
CC   -!- FUNCTION: Type II topoisomerase (PubMed:27060564, PubMed:25463606).
CC       Processively relaxes supercoiled DNA (PubMed:27060564). Displays DNA-
CC       supercoiling activity only when associated with the viral histone-like
CC       protein (PubMed:28381576). {ECO:0000269|PubMed:25463606,
CC       ECO:0000269|PubMed:27060564, ECO:0000269|PubMed:28381576}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000269|PubMed:25463606};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P11388};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P11388};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P11388};
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:0000250|UniProtKB:P11388};
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:25463606}.
CC       Note=Localizes throughout the cytoplasmic viral factories at 16 hpi.
CC       {ECO:0000269|PubMed:33429879}.
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle
CC       (PubMed:32075923). It is transcribed early, under the control of an
CC       early promoter, but its transcript levels are maintained and still
CC       present during late infection (Probable). {ECO:0000269|PubMed:32075923,
CC       ECO:0000305|PubMed:1316688, ECO:0000305|PubMed:32075923}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M88699; AAA42735.1; -; Genomic_DNA.
DR   EMBL; U18466; AAA65341.1; -; Genomic_DNA.
DR   PIR; B42549; ISXFAS.
DR   RefSeq; NP_042805.1; NC_001659.2.
DR   SMR; Q00942; -.
DR   GeneID; 22220341; -.
DR   KEGG; vg:22220341; -.
DR   Proteomes; UP000000624; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; 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   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; 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; IPR002205; Topo_IIA_dom_A.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR031660; TOPRIM_C.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF16898; TOPRIM_C; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA-binding; Early protein; Host cytoplasm; Isomerase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Topoisomerase.
FT   CHAIN           1..1192
FT                   /note="DNA topoisomerase 2"
FT                   /id="PRO_0000145388"
FT   ACT_SITE        800
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000303|PubMed:25463606"
FT   BINDING         64
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         142..149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000303|PubMed:25463606"
FT   BINDING         438
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P11388"
FT   BINDING         539
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P11388"
FT   BINDING         539
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11388"
FT   BINDING         541
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P11388"
FT   SITE            799
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         800
FT                   /note="Y->F: Complette loss of topoisomersae II activity."
FT                   /evidence="ECO:0000269|PubMed:25463606"
SQ   SEQUENCE   1192 AA;  135544 MW;  13887DB36D26C667 CRC64;
     MEAFEISDFK EHAKKKSMWA GALNKVTISG LMGVFTEDED LMALPIHRDH CPALLKIFDE
     LIVNATDHER ACHSKTKKVT YIKISFDKGV FSCENDGPGI PIAKHEQASL IAKRDVYVPE
     VASCFFLAGT NINKAKDCIK GGTNGVGLKL AMVHSQWAIL TTADGAQKYV QQINQRLDII
     EPPTITPSRE MFTRIELMPV YQELGYAEPL SETEQADLSA WIYLRACQCA AYVGKGTTIY
     YNDKPCRTGS VMALAKMYTL LSAPNSTIHT ATIKADAKPY SLHPLQVAAV VSPKFKKFEH
     VSIINGVNCV KGEHVTFLKK TINEMVIKKF QQTIKDKNRK TTLRDSCSNI FVVIVGSIPG
     IEWTGQRKDE LSIAENVFKT HYSIPSSFLT SMTRSIVDIL LQSISKKDNH KQVDVDKYTR
     ARNAGGKRAQ DCMLLAAEGD SALSLLRTGL TLGKSNPSGP SFDFCGMISL GGVIMNACKK
     VTNITTDSGE TIMVRNEQLT NNKVLQGIVQ VLGLDFNCHY KTQEERAKLR YGCIVACVDQ
     DLDGCGKILG LLLAYFHLFW PQLIIHGFVK RLLTPLIRVY EKGKTMPVEF YYEQEFDAWA
     KKQTSLVNHT VKYYKGLAAH DTHEVKSMFK HFDNMVYTFT LDDSAKELFH IYFGGESELR
     KRELCTGVVP LTETQTQSIH SVRRIPCSLH LQVDTKAYKL DAIERQIPNF LDGMTRARRK
     ILAGGVKCFA SNNRERKVFQ FGGYVADHMF YHHGDMSLNT SIIKAAQYYP GSSHLYPVFI
     GIGSFGSRHL GGKDAGSPRY ISVQLASEFI KTMFPAEDSW LLPYVFEDGQ RAEPEYYVPV
     LPLAIMEYGA NPSEGWKYTT WARQLEDILA LVRAYVDKDN PKHELLHYAI KHKITILPLR
     PSNYNFKGHL KRFGQYYYSY GTYDISEQRN IITITELPLR VPTVAYIESI KKSSNRMTFI
     EEIIDYSSSE TIEILVKLKP NSLNRIVEEF KETEEQDSIE NFLRLRNCLH SHLNFVKPKG
     GIIEFNSYYE ILYAWLPYRR ELYQKRLMRE HAVLKLRIIM ETAIVRYINE SAELNLSHYE
     DEKEASRILS EHGFPPLNHT LIISPEFASI EELNQKALQG CYTYILSLQA RELLIAAKTR
     RVEKIKKMQA RLDKVEQLLQ ESPFPGASVW LEEIDAVEKA IIKGRNTQWK FH