TOP2_IIV3
ID TOP2_IIV3 Reviewed; 1113 AA.
AC Q196X4;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=DNA topoisomerase 2;
DE EC=5.6.2.2 {ECO:0000255|PROSITE-ProRule:PRU00995};
DE AltName: Full=DNA topoisomerase II;
GN ORFNames=IIV3-086L;
OS Invertebrate iridescent virus 3 (IIV-3) (Mosquito iridescent virus).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Betairidovirinae; Chloriridovirus.
OX NCBI_TaxID=345201;
OH NCBI_TaxID=7163; Aedes vexans (Inland floodwater mosquito) (Culex vexans).
OH NCBI_TaxID=42431; Culex territans.
OH NCBI_TaxID=332058; Culiseta annulata.
OH NCBI_TaxID=310513; Ochlerotatus sollicitans (eastern saltmarsh mosquito).
OH NCBI_TaxID=329105; Ochlerotatus taeniorhynchus (Black salt marsh mosquito) (Aedes taeniorhynchus).
OH NCBI_TaxID=7183; Psorophora ferox.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16912294; DOI=10.1128/jvi.00464-06;
RA Delhon G., Tulman E.R., Afonso C.L., Lu Z., Becnel J.J., Moser B.A.,
RA Kutish G.F., Rock D.L.;
RT "Genome of invertebrate iridescent virus type 3 (mosquito iridescent
RT virus).";
RL J. Virol. 80:8439-8449(2006).
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}.
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DR EMBL; DQ643392; ABF82116.1; -; Genomic_DNA.
DR RefSeq; YP_654658.1; NC_008187.1.
DR SMR; Q196X4; -.
DR PRIDE; Q196X4; -.
DR GeneID; 4156297; -.
DR KEGG; vg:4156297; -.
DR Proteomes; UP000001358; 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..1113
FT /note="DNA topoisomerase 2"
FT /id="PRO_0000377770"
FT DOMAIN 441..563
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT ACT_SITE 789
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 150..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 162..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 371..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 447
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 532
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 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT BINDING 534
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 788
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1113 AA; 126321 MW; 89980A19B1320181 CRC64;
MAPKNHQKYT IKNDIQHVLD CSDVYIGDTA PTARSEWMFD DAVNQIVWRP TTTPEALVRI
FVEVLTNAVD NIERSINGGH ELCKNIKVDV DLKTGKTSVW NDGQVIPVVK NCDNGVVQPP
PPTTEQDRLA YEKLNREYIH TIIFGHFRTS SNYDNETDQV SGKNGVGVKC TNIFSSWFSV
VGVDPDRKLK FSQEWRSNMT KSGAPQVVKC ALKTGYTLVE YVPDFARFKL KSYPEDVESI
FKKLVVDASA FFPNTAFFFN GERTVVKNAV AYAKLYYNLN ETAVDSVVID YKDSKVVVVG
SATPLPPVSF VNGQITPAGG QHVTNWSRVI FGALLAALNG KKNVSLTKAD IAPYFQLFIH
SKVSKPKFDG QNKNCLKSPK VEAHLDATIL KKMLKWKIIS TIQDKVVKSK EYLALKKIEC
RRTPIVKVDG YDQANRLGPD SVLIVCEGLS AKSYAVAGIQ KGLFNKKGRT YFGILPLRGK
FLNVKNTTPL KIGQNKVVSD FIKVLNLKFN LDYRKATNYA TLNYGTLLIL TDADKDGIHI
KGLILNLIHE LFPTLFHRQG FIYSMETPIV KILHKKGQPT LFYDENSFED WRAQHPELKH
FKYYKGLGTI GPADVAAFFG SKVVRYHYDE ATDAAVNSVF KDENANERKE WLGRFNPRVS
QWCLDHHREA VIDLKISDFM HHEMIKFSYE DCRRSLASCI DGFKESQRKI IYAVRKKFRS
NSTEFIKVAQ LSGYVAEQTD YKHGEQNLCE TIVKFAQDFV GANNVQLLEP DGQFGTRLEG
GKDSAAPRYI YTKPHKILPY IFREEDDPIL EQSSEGEPVH FVPIIPLVLV NGSVGIGTGW
SCFVPQYNPL ELIRYIEARL TSQDSEALLP AKPWYRNFTG KVAATGPGKF TTFGRMKQVD
ADTVRVTELP VGMWTDRFKD QCYSLIESGQ LQQLVNESTV SKVDFTLKKL QDISALKLTT
TLHTTNMVLF DRENVITKYD TIGDILDHYF QTRLAFYKVR KNHTIAQLKN TIQHNETKLK
FIEKVLTDHS FLRQDDAAIV SILEKENFLK VDNSYNYLLN ISIRSCTATA VEKLQSTIKG
LTESLIRVQQ TPTRQMWYDE LQQLKQVGNW SEP
