ID A0A1I7TBD9_9PELO Unreviewed; 1108 AA.
AC A0A1I7TBD9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold571.g4285.t1};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold571.g4285.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- FUNCTION: Control of topological states of DNA by transient breakage
CC and subsequent rejoining of DNA strands. Topoisomerase II makes double-
CC strand breaks. {ECO:0000256|RuleBase:RU362094}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185,
CC ECO:0000256|RuleBase:RU362094};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080, ECO:0000256|RuleBase:RU362094}.
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 AlphaFoldDB; A0A1I7TBD9; -.
DR STRING; 1561998.A0A1I7TBD9; -.
DR WBParaSite; Csp11.Scaffold571.g4285.t1; Csp11.Scaffold571.g4285.t1; Csp11.Scaffold571.g4285.
DR Proteomes; UP000095282; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.1490.30; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_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; IPR001154; TopoII_euk.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR PRINTS; PR01158; TOPISMRASEII.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362094};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362094};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362094};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362094};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 414..528
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1066..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1086
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1108 AA; 127548 MW; D6D2598F88C9F301 CRC64;
MHRIRILTRL AIFYKRPSQF KRIRSFCFHI PSTSFSSEAA SKYEKKSPIE HVLLRPDTYI
GGVGMREIET VWMKNEGEFK REITSREVTY PPGLLKIFDE ILVNAADNKS RDPKMNRLEV
WLDRETPRIS VWNNGIGLPV EIHPSENIYV PSLVFGNLFT SSNYNDSEVK TVGGRNGYGA
KLCNIFSKEF IVETVDSNTK RRFKQVEFVP DLERFHINEM SDDIVQMIEK RVFEVAATLP
NNVDVFFNGQ KCDVDGFEDY VKMFNASDPS SFLFLHPTSR WHVGVAKRVF HMEENQINFP
KVVSFVNNIN TEKGGTHVDY VMDKLVNILK PMVDSKLKDT GRSVKPAFIK NHLSVFINCL
IENPSFESQT KETVTTKPKH FGSIFDCDSV VREYYIVKLE DAEWAGISGK SDKCTLILTE
GDSAKALALA GLEVLGREKY GVFPLKGKLI NVSNLDEIRA SKNEEISNLV RILGLNFNDP
SPSHQSIRYG RLLILSDQDE DGSHIKGLVI NFIHKFWPTL IHSGDFIQSF RTPLLKAKKG
DEIKSFFSMN EYKKWAESSE GKWKIKYYKG LGTSTSNEAR EYFSNLDHHI VNFKYTGTTD
DESIRMVFDR ERSDERKIWI RKFEENVAED PEIDAKNEIS YEEFVDGQLM EFGMIDLKRS
IPSLVDGLKP SQRKVLWTLL NMDESIEMKV SQLAGAVAHR QSYHHGEESL LRTIIRMGQS
FCGSSNLPLL QPIGQFGTRH EGGNDAASAR YIFTSLAPTT RLLFPRSDDD LLIKNVEEGM
IVEPKWLCPI IPLILVNGTE GIGTGWSTKI ANRNPIDTIG LIRKRIDSED INEDISPFYQ
DYNGKIEVVN STKFTSSGKI KIIRPERINA SSFSIDITEL PIGIWTSKYK EKLSKIMENL
PVTEFSEKHS EKRVHFHLSV DRKKASRFLQ KSNSDLLNYF KLRTSITENR VLFNENCQLK
EYGTVSEIVS EFFNIRRNLY ERRLEIQREE CVSKLKYVDN QIKFIDLVTN GTIELRSMGR
EQLEEKLEHL EFETDPLVSK SKMKTSKKSR DYNYLLEMPL SRLTSDEMNR LNEKREKRKK
DLETAESADW QSTWHNELDK LAAGIKKN
//
