ID A0A098VQW0_9MICR Unreviewed; 1211 AA.
AC A0A098VQW0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=DI09_87p90 {ECO:0000313|EMBL:KGG50136.1};
OS Mitosporidium daphniae.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Mitosporidium.
OX NCBI_TaxID=1485682 {ECO:0000313|EMBL:KGG50136.1, ECO:0000313|Proteomes:UP000029725};
RN [1] {ECO:0000313|EMBL:KGG50136.1, ECO:0000313|Proteomes:UP000029725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UGP3 {ECO:0000313|EMBL:KGG50136.1,
RC ECO:0000313|Proteomes:UP000029725};
RC TISSUE=Spores {ECO:0000313|EMBL:KGG50136.1};
RA Haag K.L., James T.Y., Larsson R., Schaer T.M., Refardt D., Pombert J.-F.,
RA Ebert D.;
RT "A new species of microsporidia sheds light on the evolution of extreme
RT parasitism.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGG50136.1}.
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DR EMBL; JMKJ01000598; KGG50136.1; -; Genomic_DNA.
DR RefSeq; XP_013236572.1; XM_013381118.1.
DR AlphaFoldDB; A0A098VQW0; -.
DR GeneID; 25260986; -.
DR VEuPathDB; MicrosporidiaDB:DI09_87p90; -.
DR HOGENOM; CLU_001935_1_1_1; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000029725; Unassembled WGS sequence.
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; cd00187; TOP4c; 1.
DR CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 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; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
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 InterPro; IPR034157; TOPRIM_TopoII.
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; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR PRINTS; PR01158; TOPISMRASEII.
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 Reference proteome {ECO:0000313|Proteomes:UP000029725};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 275..384
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1001..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1054
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT UNSURE 89
FT /note="E or Q"
FT /evidence="ECO:0000313|EMBL:KGG50136.1"
SQ SEQUENCE 1211 AA; 134515 MW; 527B30EDF413A717 CRC64;
MSVMEKPIIT PLLAKGTNKT DGKQFTRISF IPDLSKFKCN EKSIDQGHLS LFYRRVFDLA
GTVKGISVFL NGKKIPISSF SSYARMYVES CAFGRGEPIE SPLPLFHITV NDRWDVAVAS
SEEQFQQVSF VNSIHTSKGG THVSLITDQL VSAISDALVK KNKGMSIKPF QVKSRLWVFV
NCLIENPTFD SQTKETLTLR AAAFGSECQL PASFLTKIIN NSGIVAMLQA EFLAAAKAKE
DKELKKTDGR KSARLSGIPK LDDANFAGTK SASKCTLILT EGDSAKALAV SGLSVVGRDY
FGVYPLRGKL LNVRDANENV EISAIKQILG LQHGRVYANN DALRYGRIML MTDQDHDGSH
IKGLLINFID FFWPSLLKLP SGFLTAFITP IVVVTPKNRN SRPNRQISGV GIGARIDSTT
GAISFYTIPE YENWKTIQTT HSLSLFLIKY YKGLGTSTSA DAKKYFSSMN LHAKPFVSMT
KADARKEWLH AFVPGTFLDC STPQFTIEDF VQRELILFSM ADNVRSIPSV IDGLKPGLRK
ILFSCFKRKL KQEIKVAQLA GYVSEHAAYH HGEASLCASI IGLAQDYTGS NNIPLLVPSG
QFGTRLQGGK DAASPRYIFT CLSEISRLIF MESDDDLLVY LNDDGQSIEP EWYMPIIPML
LVNGSEGIGT GWSTFIPPFS PLEVIENVLR KIEEKPLVEM HPWYRCFSGS ILCSESMGYK
IYGKANLRYV CTDWVLNITE LPVGVWTQNY KEFLESLIER SPALVKEFTE HHTDTCVSFS
IKLGEAAIES AEAILDPHLV PSTNIATESF LKLFKLSSSI SLTNMVAFDA GGHLKRYGSA
LEILEDWYLV RLNGYHRRKE NLVSHLSREW KRLDAKMRFI SEILQGTLVI ARKSKADLVR
ELSEKGYEED ENGGGYDYLL GMPLWSLTAE RILQLENERK EKEDELKLLL SKTPCDLWKT
DLMTLKKFVS SSEYYSDHIG VRADVASQQI AYTEGEKPMK IIKLEQKEDP LRESKEPKET
EKKPIPRNAK TSAHKKTSKP MQAKESKSMQ AKKTKSLELN RAIGMVSSSE SNPPTELTAS
ASDPSITNQV PSPRTNNNSL LDRIQTMLSS SNISSAQATL SSPGINLAVN QSQHAATNVL
PKTQRKPAKK SGSNSRDAGK SQLTLDISPV IRKPSSAKNI LRRGIIKDDS SENESIASTD
GEDPFHGSTE N
//
