TOP2_ASFM2
ID TOP2_ASFM2 Reviewed; 1191 AA.
AC P34203;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000250|UniProtKB:Q00942};
DE EC=5.6.2.2 {ECO:0000250|UniProtKB:Q00942};
DE AltName: Full=DNA topoisomerase II;
GN OrderedLocusNames=Mal-120; ORFNames=i7R;
OS African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10500;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1335084; DOI=10.1016/0022-2836(92)90887-p;
RA Baylis S.A., Dixon L.K., Vydelingum S., Smith G.L.;
RT "African swine fever virus encodes a gene with extensive homology to type
RT II DNA topoisomerases.";
RL J. Mol. Biol. 228:1003-1010(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8021596; DOI=10.1099/0022-1317-75-7-1655;
RA Dixon L.K., Twigg S.R.F., Baylis S.A., Vydelingum S., Bristow C.,
RA Hammond J.M., Smith G.L.;
RT "Nucleotide sequence of a 55 kbp region from the right end of the genome of
RT a pathogenic African swine fever virus isolate (Malawi LIL20/1).";
RL J. Gen. Virol. 75:1655-1684(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Type II topoisomerase. Processively relaxes supercoiled DNA.
CC Displays DNA-supercoiling activity only when associated with the viral
CC histone-like protein. {ECO:0000250|UniProtKB:Q00942}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000250|UniProtKB:Q00942};
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:0000250|UniProtKB:Q00942}.
CC Note=Localizes to the cytoplasmic viral factories.
CC {ECO:0000250|UniProtKB:Q00942}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
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DR EMBL; Z14245; CAA78614.1; -; Genomic_DNA.
DR EMBL; X71982; CAA50820.1; -; Genomic_DNA.
DR EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S27329; S27329.
DR SMR; P34203; -.
DR Proteomes; UP000000860; 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; 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; 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 3: Inferred from homology;
KW ATP-binding; DNA-binding; Early protein; Host cytoplasm; Isomerase;
KW Magnesium; Metal-binding; Nucleotide-binding; Topoisomerase.
FT CHAIN 1..1191
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000145389"
FT ACT_SITE 799
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q00942"
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:0000250|UniProtKB:Q00942"
FT BINDING 437
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 538
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 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT SITE 798
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 421
FT /note="A -> AR (in Ref. 3; AY261361)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="V -> L (in Ref. 3; AY261361)"
FT /evidence="ECO:0000305"
FT CONFLICT 1040..1041
FT /note="DV -> EL (in Ref. 3; AY261361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1191 AA; 135071 MW; 62858BFF3F67CE22 CRC64;
MEAFEISDFK EHAKKKSMWA GALNKVTISG LMGVFTEDED LMALPIHRDH CPALLKIFDE
LIVNATDHER ACHSKTKKVT YIKISFDKGV FACENDGPGI PIAKHEQASL IAKRDVYVPE
VASCHFLAGT NINKAKDCIK GGTNGVGLKL AMVHSQWAIL TTADGAQKYV QHINQRLDII
EPPTITPSRE MFTRIELMPV YQELGYAQPL SETEQADLSA WIYLRACQCA AYVGKGTTIY
YNDKPCNTGS VMALAKMYTL LSAPNSTIHT TAIKADAKPY SLHPLQVAAV VSPKFKKFEH
VSIINGVNCV KGEHVTFLKK TINEMVVKKF QQTIKDKNRK TTLRDSCSNI FVVIVGSIPG
IEWTGQRKDE LSIAENVFKT HYSIPSSFLT NMTRSIVDIL LQSISKKDNH KQVDVDKYTR
ANAGGKKAQD CMLLAAEGDS ALSLVRAGLT LGKSNPSGPS FDFCGMISLG GVIMNACKKV
TNITTDSGET IMVRNEQLTN NKVLQGIVQV LGLDFNCHYK TQEERAKLRY GCIVACVDQD
LDGCGKILGL LLAYFHLFWP QLIIHGFVKR LLTPLIRVYE KGKTVPVEFY YEQEFDAWAK
KQTSLANHTV KYYKGLAAHD THEVKSMFKH FDNMVYTFTL DDSAKELFHI YFGGESELRK
RELCTGVVPL TETQTQSIHS DRQIPCSLHL QVDTKAYKLD AIERQIPNFL DGMTRARRKI
LAGGLKCFAS NNRERKVFQF GGYVADHMFY HHGDMSLNTS IIKAAQYYPG SSHLYPVFIG
IGSFGSRHLG GKDAGSPRYI SVQLASEFIK TMFPAEDSWL LPYVFEDGQR AEPEYYVPVL
PLAIMEYGAN PSEGWKYTTW ARQLEDILAL VRAYVDKNNP KHELLHYAIE RKITVLPLRP
SNYNFKGHLK RFGQYYYSYG TYVVSEQRNI ITITELPLRV PTVAYIESIK KSSNRMAFIE
EIIDYSSSET IEILVKLKPN SLNRIVEEFK ETEEQDSIEN FLRLRNCLHS HLNFVKPKGG
IIEFNSYYEI LYAWLPYRRD VYQKRLMRER AVLKLRIIME TAIVRYINES ADLNLSHYED
EKEASRILSE HGFPPLNQSL ITSPEFASIE ELNQKALQGC YTYILSLQAR ELLIAAKTRR
VEKIKKMQAR LDKVEQLLQE SPFPGASVWL EEIDAVEKAI IKGRSTQWKF H
