ID A0A2C9K9W2_BIOGL Unreviewed; 852 AA.
AC A0A2C9K9W2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN Name=106064485 {ECO:0000313|EnsemblMetazoa:BGLB016827-PA};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB016827-PA, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB016827-PA}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB016827-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363039}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {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 RefSeq; XP_013078504.1; XM_013223050.1.
DR AlphaFoldDB; A0A2C9K9W2; -.
DR STRING; 6526.A0A2C9K9W2; -.
DR EnsemblMetazoa; BGLB016827-RA; BGLB016827-PA; BGLB016827.
DR VEuPathDB; VectorBase:BGLB016827; -.
DR OrthoDB; 5404194at2759; -.
DR Proteomes; UP000076420; Unassembled WGS sequence.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
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 GO; GO:0006418; P:tRNA aminoacylation for protein translation; IEA:InterPro.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR006691; GyrA/parC_rep.
DR InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 5.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 2.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 2.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363039};
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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363039};
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 Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363039};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 145..509
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
SQ SEQUENCE 852 AA; 95670 MW; 16300A6860EFE8AD CRC64;
MEYTSSSIKI LEGLEAVRKR PVNDINVELA LQHVDTEDYV VASFCNNIST HEGGTHEEGF
KMAFTRVINN YLTTNFKKSK DKINLQGEDI REGLTCLISI KHPEPQYEGQ TKGKLSNSDA
RKAVNDLFDV NFEKFLLENP EVANKIIEKG LEAQRARIAA KKAREFVKRK GVLEISTLPG
KLADCSSRNP KECELFLVEG DSAGGSAKLG RNREIQAILP LKGKVINVEK NLIQKIMNNQ
EIGNLIKSIG CGIQESFDIA GIAVGMATNI PPHNLNNVID ALILQINDDS VDIEKLIDAI
QGPDFPTGGY VSSPSNIRKI YRDGSGSVTI QAKVDVLEEE RILIVKEIPY QTNKARIIER
IAELVNDKII EGISDIKDES NYEGIRIVIK YKKGFESEVE ILVKKTRFEL KAAEQRIHLL
LGIKKAVEDI DKTVRILKES RTSSDAISNL CDQLEITQVQ AKAILDMKMQ RLVEKFGDER
RSEITEDYSN IEDEDLIKRE DIVVLMTQSN YIKRIPVEEY KLQNRGGVGT KSLSFYEDDV
TKLVTSGSTH DDYMFFTKKG FVYRIKGYKI FSKSKQSKGI PIINLLKTLE KDDDIKEIIN
VSKEDYNANT SLSFITKTGL IKKTSILHYA RINVNGKIAI SLRENDEIVN VLKTTKETKC
IVVTSNGKGL RFDASLIRDI GRSSQGVKAI KLLDNSYVVS AANDSNSKYL LIITEKGMGK
LNLLDEGFRI KGRGTQGYNL ISKSNNDRIV YSLSVNENDE ILLVTEKVYI TTPIYYPNST
LHIGHAYSTV IADSYKRFRI NTGDDVYFLT GSDEHVTVNN EKMSKSLGNV VNPLELIDKY
GADSLRYFLM KS
//
