ID A0A317WQG5_9EURO Unreviewed; 1781 AA.
AC A0A317WQG5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|ARBA:ARBA00019635, ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895, ECO:0000256|RuleBase:RU362094};
GN ORFNames=BO70DRAFT_178864 {ECO:0000313|EMBL:PWY88305.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY88305.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY88305.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY88305.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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:PWY88305.1}.
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DR EMBL; MSFL01000005; PWY88305.1; -; Genomic_DNA.
DR STRING; 1448321.A0A317WQG5; -.
DR VEuPathDB; FungiDB:BO70DRAFT_178864; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000247233; 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 GO; GO:0061982; P:meiosis I cell cycle process; IEA:UniProt.
DR CDD; cd16930; HATPase_TopII-like; 1.
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; 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 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; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR PRINTS; PR01158; TOPISMRASEII.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000247233};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 550..664
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1272..1723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1740..1781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1111..1142
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1741..1755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1781 AA; 198334 MW; B3A0126271484ABB CRC64;
MDDSMVESAF EDEDVSDFLP EPAPKPKAKA APKKKLTQTK LTAKPTAKAA SKKRAKPDTD
DEIDDGDDNI SGDDSVLSHT PPKKAKKAAA PAKKAGSKPL ADLENESFGK DGSVEPAKGT
DVSEKYQKLT QLEHIIKRPD TYIGSIERTL QQMWVYSSET EGMEFREVSY VPGLYKIFDE
IVVNAADNKQ NDAGMDEIRV TVDRESGVIS VWNNGRGIPI EMHSKEKIYV PELIFGHLLT
SSNYDDTQQK VTGGRNGFGA KLCNVFSTEF SIETQDSRQK KKYRQTWTDN MTKMGKAKIT
EAKGDDYTKV TFKPDYAKFG MDGMDDDFEA LVKRRVYDLA GTAKVAVKLN GTRVPIRNFR
KYMEMYTKAI RKERGDNGPA AKDEIITCSP DPHWEIGFAV SDGSFQQVSF VNSIATTSGG
SHVNYIADQI CNKLADQVKK KNKNGATLKT AQIRNHIFIF VNALVVNPAF TSQTKEQLTT
KQSQFGSKCV LEEDFYKKVL KTEVMSNILH FAQQKADQML KKTDGGRRSR MNNPKLTDAN
KAGTKDGHHC TLILTEGDSA KGLAMAGRAV VGPDLFGVFP LRGKLLNVRD ASFDQISKNA
EIQNIKNFLG LQHKKEYTET RGLRYGHLMI MTDQDHDGSH IKGLLINFLQ AQFPSLLKIP
EFLIEFITPI VKIWKGDPKN PTKQRSFFTM PEYEAWREDH KDERGWDHKY YKGLGTSTTE
DAQVYFRDLD RHLKEFHTMQ DNEAELIELA FSKKKADERK EWLRQFKPGT FLDHSVEKIT
YTDFINKELI LFSMADNIRS IPSVVDGLKP GQRKVLYTCF RRNLKKDMKV VELAGHVSGM
TAYQHGDTSL QQTIVGLAQT FVGSNNINCL EPSGNFGSRL QGGSDCASAR YIYTRLSPFA
RRIFQTADEP LLTYNEDDGK KIEPEVYMPV VPMILVNGAD GIGTGWSSSI PNYNPEDIVD
NLNRLMDGEE LKPMQPWFRG FTGEVTAIGG DRFKFSGIIK ETGEKEVEIT ELPIRTWTQD
FKDKLEDIIK AEKTPSFIKD YRDYNTHTKV HFVIQMDEKH MKSAVTDGLE EKFKLTKTIA
TTNLVAFDPE GRITKYATVD DILKEFFHLR LKFYERRKQH QLNELQKELE KLSNQARFVQ
MIIDGELVVS KKKKTVLVVE LKEKGFKPFP KVAEAHKAGE MEPAMEDEEE DPETSPDTEN
LSNAYDYLLG MAIWSLTQER VERLRRQIGE KEVDIDTLIK LSKEDIWKKD LEDFINEWRF
QLEDEARRMR KVQNMGRRTS AKLMTTTGRG GGRKRKVADD DDEDFGVPKT KRGPKKAEPK
GTLHNFLKKP SPKPAVKDGD SDDDFDFDME VMPKKSRGSA KPTPQPKEEE TADSDVEIVP
KKSRAAPKSK AKEEDTDASE VKPAPKRGRA AAKPKAKSAD DDMDDDDFME IAKAQAAEAA
PPTSRARKPA KYTMSDSESD NGDDLLGDVS KMVKGIGGTA GGSTSDRQLF SERSQIGGSS
GLPTSSKPSK PSPDFDADET DYSKLVPQSS PRRSLHVKSK DTKVLDDSED EEEPVKPAAS
KAKPAARGKA AAKVFEFSDE DEEEPVKPAA TKAKPAARGK AAAAKPAANV FEFSDDDEEE
EEPVKPAATK AKPAARGKAA STVLDDSDIE EEEPVKPAAT KAKPAARGKA AAAKPAPKAR
GRPKKDAVSA VAAEKPAALS PAAKAYASKQ AKTTAANKKK QLADDLSDDD IDAMANDILD
SPAAATTSRP ARRTATAQKK TYVIDDDSEG DSGDDFEEDS E
//
