TOP2_ASFWA
ID TOP2_ASFWA Reviewed; 1192 AA.
AC P0C9C1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
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=War-122;
OS African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561444;
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 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; AY261366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C9C1; -.
DR Proteomes; UP000000858; 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 3: Inferred from homology;
KW ATP-binding; DNA-binding; Early protein; Host cytoplasm; Isomerase;
KW Late protein; Magnesium; Metal-binding; Nucleotide-binding; Topoisomerase.
FT CHAIN 1..1192
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000373131"
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; 135414 MW; 00FCDEA50957600C CRC64;
MEAFEISDFK EHAKKKSMWA GALNKVTISG LMGVFTEDED LMALPIHRDH CPALLKIFDE
IIVNATDHER ACHSKTKKVT YIKISFNKGV FSCENDGPGI PIAKHEQASL IAKRDVYVPE
VASCHFLAGT NINKAKDCIK GGTNGVGLKL AMVHSQWAIL TTADGAQKYV QHINQRLDII
EPPTITPSRE MFTRIELMPV YQELGYAEPL SETEQADLSA WIYLRACQCA AYVGKGTTIY
YNEKPCRTGS VMALAKMYTL LSAPNGTIHT ATIKADAKPY SLHPLQVAAV VSPKFKKFEH
VSIINGVNCV KGEHVTFLKK TINEIVVKKF QQTIKDKNRK TTLRDSCSNI FIVIVGSIPG
IEWTGQRKDE LSIAENVFKT HYSIPSSFLT SMTKSIVDIL LQSISKKDNH KQVDVDKYTR
ARNAGGKRAQ DCMLLAAEGD SALSLLRTGL TLGKSNPSGP SFDFCGMISL GGVIMNACKK
VTNITTDSGE TIMVRNEQLT NNKVLQGIVQ VLGLDFNCHY KTQEERAKLR YGCIVACVDQ
DLDGCGKILG LLLAYFHLFW PQLIIHGFVK RLLTPLIRVY EKGKTVPVEF YYEQEFDAWA
KKQTSLANHT 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 LVRAYVDKNN PKHELLHYAI KHKITILPLR
PSNYNFKGHL KRFGQYYYSY GTYVISEQRN IITITELPLR VPTVAYIESI KKSSNRMTFI
EEIIDYSSSE TIEILVKLKP NSLNRIMEEF KCTEEQDSIE NFLRLRNCLH SHLNFVKPKG
GIIEFNTYYE ILYAWLPYRR ELYQKRLMRE HAVLKLRIIM ETAIVRYINE SAELNLSHYE
DEKEASRILS EHGFPPLNQT LIISPEFASI EELNQKALQG CYTYILSLQA RELLIAAKTR
RVEKIKKMQA RLDKVEQLLQ ESPFPGASVW LEEIDAVEKA IIKGRNTQWK FH
