TOP2_IIV6
ID TOP2_IIV6 Reviewed; 1132 AA.
AC Q9QSK1;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
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; ORFNames=IIV6-045L;
OS Invertebrate iridescent virus 6 (IIV-6) (Chilo iridescent virus).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Betairidovirinae; Iridovirus.
OX NCBI_TaxID=176652;
OH NCBI_TaxID=6997; Acheta domesticus (House cricket).
OH NCBI_TaxID=168631; Chilo suppressalis (Asiatic rice borer moth).
OH NCBI_TaxID=6999; Gryllus bimaculatus (Two-spotted cricket).
OH NCBI_TaxID=58607; Gryllus campestris.
OH NCBI_TaxID=7108; Spodoptera frugiperda (Fall armyworm).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11448171; DOI=10.1006/viro.2001.0963;
RA Jakob N.J., Mueller K., Bahr U., Darai G.;
RT "Analysis of the first complete DNA sequence of an invertebrate iridovirus:
RT coding strategy of the genome of Chilo iridescent virus.";
RL Virology 286:182-196(2001).
RN [2]
RP GENOME REANNOTATION.
RX PubMed=17239238; DOI=10.1186/1743-422x-4-11;
RA Eaton H.E., Metcalf J., Penny E., Tcherepanov V., Upton C., Brunetti C.R.;
RT "Comparative genomic analysis of the family Iridoviridae: re-annotating and
RT defining the core set of iridovirus genes.";
RL Virol. J. 4:11-11(2007).
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}.
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; AF303741; AAD48151.1; -; Genomic_DNA.
DR RefSeq; NP_149508.1; NC_003038.1.
DR SMR; Q9QSK1; -.
DR PRIDE; Q9QSK1; -.
DR GeneID; 921682; -.
DR KEGG; vg:921682; -.
DR Proteomes; UP000001359; 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 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; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR Pfam; PF00204; DNA_gyraseB; 1.
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; 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..1132
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000377771"
FT DOMAIN 442..577
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 327..329
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT REGION 979..988
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT ACT_SITE 803
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P06786"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 100
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 363..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT BINDING 448
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 538
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 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 486
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 489
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT SITE 666
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT SITE 667
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT SITE 721
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT SITE 755
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
FT SITE 802
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 934
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P11388"
SQ SEQUENCE 1132 AA; 129877 MW; 4626121A5FCC6201 CRC64;
MATSNHKKQY TTLSDIDHVL LRPEVIIGST VPMEQTEYVV DENFSEILEK QVFVSEALIR
IFVEVLANAV DNIHRSKGSS TPCKSIKIKI EDDGTTMIHN DGQVIKISKE ENDGIEINGK
KCSVYNHELV FGHLRSSSNY DDTVVRQTSG KNGLGVKCTN ILSKSFKVIG VDPENKKKFV
QEWTNNMKET SGPKVTTSSS KTGYTEVIYC PDFERLGNFS SDIIGIFRKH VLDVAMLASS
EGVSVYFNDK KLPIKKFSDY TKLFKLEKES ISITEEDGSS EVTIAFVERD GKKKPISFVN
GLFTKHGGQH VDGWTKPFFA NLLSVLNKPS KTYKDLKLSL KDVTPYFRFF VKSTVDKPQF
DCQNKNMLKS PCLKYTIPDK IITKVCKWTS VQELKQSSFE KLLKGKDNNI IKTLNDKKRR
PKVSVKEYDP ANKAGTTLSE KCTLIVCEGL SAKTYAVAGI STGISFTGTD TKKGRDWFGI
LPLRGKFLNV RNANNDKMIK NTVVTDLVNA MGLTFGMDYS TQKSRKSLNY GSIIIIPDPD
EDGIHIEGLV LNFFHHHFSS LFNPVVPNLK DFPFISSMKI PIIKVIEKPL KGRREIEFFT
HEAFHKFKNE NKWHKNHEIK YFKGLGTTKH EDVPKIFGKK MVVFNIDDNA HENMEKAFKD
EEADERKEWL KQYNPNARTF DLDSPNKILQ LNISTFINEE LIKFSIEDCK RSLPHLIDGL
KESQRKVIFG LKQWNGKNNI KVAQLGAFVA QKTDYKHGEQ NLFDTIIKMA QTFVGANNIP
LLEEDGQFGT RLSGGKDAAS PRYIFVNQPP ILNKIFRPED DPILNYTLDG EPVFYAPVIP
LICINGSVGV GTGFSCNIPM FNPSEIIDGL KQWINMREQG EKYVFKYKPW YKGFTGKIEK
NGSGRYISYG TLSNEASNNG MYQYTVSELP INMWTDKFKE MCDQYRESNL IKTCDNYSEV
TTVNFKISSE HELTIENLKL RSYIHTSNMV MFDHEGKIHK YETLNGIMQR FCKERIKIYE
KRRQYMLQKL NKSLTISENK KRFMEDVMNQ KIKILLQEDE VVHQQLLDMN YYKDDEGEFD
YLLNMNIGGF RKKNVDKLIS KIDDLKKDIM WYTNTNEGQM WLKDILELEP FI
