TOP2_ASFK5
ID TOP2_ASFK5 Reviewed; 1192 AA.
AC P0C9C2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 55.
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=Ken-124;
OS African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561445;
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 [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 throughout the cytoplasmic viral factories at 16 hpi.
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; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C9C2; -.
DR PRIDE; P0C9C2; -.
DR Proteomes; UP000000861; 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; 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; 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; SSF54211; SSF54211; 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; Host cytoplasm; Isomerase; Late protein;
KW Magnesium; Metal-binding; Nucleotide-binding; Topoisomerase.
FT CHAIN 1..1192
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000373132"
FT ACT_SITE 800
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 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"
SQ SEQUENCE 1192 AA; 135365 MW; 878799A05F377306 CRC64;
METFEISDFK EHAKKKSMWA GALNKVTISG LMGVFTEDED LMALPIHRDH CPALLKIFDE
LIVNATDHER ACHNKTKKVT YIKISFDKGV FSCENDGPGI PIVKHEQASL IAKRDVYVPE
VASCYFLAGT NINKAKDCIK GGTNGVGLKL AMVHSQWAIL TTADGAQKYV QHINQRLDNI
EPPTITPSRE MFTRIELMPV YQELGYAQPL SETEQADLSA WIYLRACQCA AYVGKGTTIY
YNDKPCSTSS VMALAKMYTL VTAPNSTIYT TTIKADAKPY SLHPLQVAAV VSPKFKKFEH
VSIINGVNCV KGEHVTFLKK AINEMVVKKF QQTVKDKNRK TTLRDSCSNI FVVIVGSIPG
IEWTGQRKDE LSIAENVFKT HYSIPSSFLT SMTRSIVDIL LQSISKKDNH KQIDVDKYTR
ARNAGGKKAQ DCMLLAAEGD SALSLLRAGL TLGKSNPSGP SFDFCGMISL GGVIMNACKK
VTNITTDSGE TIMVRNEQLT NNKVLQGIVQ VLGLDFNCHY KTQEERAKLR YGCIVACVDQ
DLDGCGKILG LLLAYFHLFW PQLIVHGFVK RLLTPLIRVY EKGNTVPVEF YYEQEFDAWA
KKQTSLANHT VKYYKGLAAH DTHEVKSMFK HFDKMVYTFT LDDSAKELFH IYFGGESELR
KRELCTGVVP LTETQTQSIH SVRRIPCSLH LQVDTKAYKL DAIERQIPNF LDGMTRARRK
ILAGGLKCFA SNNRERKVFQ FGGYVADHMF YHHGDMSLNT SIIKAAQYYP GSSHLYPVFI
GIGSFGSRHL GGKDAGSPRY ISVQLASEFI KTMFPAEDSW LLPYVFEDGQ RAEPEYYVPV
LPLAIMEYGA NPSEGWKYTT WARQLEDILA LVRAYIDKNN PKHELLHYAI DHKITVLPLR
PSNYNFKGHL KRFGQYYYSY GTYVVSEQRN MITITELPLR VPTVAYIESI KKSSNRMAFI
EEIVDYSSSE TIEILVKLKP NSLSRIIEEF KETEEQNSIE NFLRLRNCLH SHLNFVKPKG
GIIEFNSYYE ILYAWLPYRR DLYQKRLMRE RAVLKLRIIM ETAIVRYINE SADLNLSHYE
DEKEAGRILS EHGFPPLNQS LITSPEFATI EELNQKALQG CYTYILSLQA RELLIAAKTR
RVEKIKKMQA RLDKVEQLLQ ESPFPGASVW LEEIDAVEKA IIKGRNTQWK FH
