ID A0A0A2VX67_BEABA Unreviewed; 1605 AA.
AC A0A0A2VX67;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=BBAD15_g2043 {ECO:0000313|EMBL:KGQ12203.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ12203.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ12203.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ12203.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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:KGQ12203.1}.
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DR EMBL; ANFO01000134; KGQ12203.1; -; Genomic_DNA.
DR STRING; 1245745.A0A0A2VX67; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_2_0_1; -.
DR Proteomes; UP000030106; 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 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:UP000030106};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 546..664
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1508..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1584..1605
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1605 AA; 179622 MW; D0A77401C67D203A CRC64;
MDSDMMDDDV FSPDNESDGY VPEPKKTKPA ASKAKKLTQT TLKPKAPAKK RKVISDDEDD
DNDSMGFSNT PPSSKKTKKA PPAKKSSGVP LAELENDSMV VDSTPKPAGK KKSATETYQK
LTQLEHIIKR PDTYIGSVES TEQQMWVYNK EAQLMEYKTI SFVPGFFKIF DEIMVNAADV
KQRHASMTYI KVNIDRESGQ ISVENNGKGI PVEMHDKEKI YIPELIFGHL LAGSNFDDEE
KKTVGGRNGY GAKLCNVFST EFNLECQDST NGKRYKQTWT DNMSKMGKAK ITSNKTSDFV
RITFMPDYKR FGMSDGIDDD LESLLYRRVY DLAGTIRGIK VHLNGEVIKI PTFKAYCDLY
AKSIAKERVA EEGGNPTCNV EIDKEKTHPR WEVGFAVSDG TFQQVSFVNN IATTSGGTHV
NYIADQITAS LLKTLNKRKK GHTLKQSHLR NHIFIFINCF IDNPAFTSQT KEQMTTKASL
FGSKCVLGEQ FLKKIAQSEA VQNIMDFAEK KADKMMAKSD GSKRSRVSNA KLVEANLAGS
RRGHECTLIL TEGDSAKGLA VSGRAILDPD RIGVFPLRGK LLNVRDASID QITKNQEIQN
IKQFLGLKHK QNYTDTKSLR YGHLMIMADQ DHDGSHIKGL LINFLQVQFP SLLQIPDFFR
EFVTPIMKVW QGSDPKKPTK LQTFFTQPEF SEWKESHKHE LSRWHSKYLK GLGSSSNEDA
QVYFTNLDKH LKEFEVMRPE EAQLFDLAFS KKRADARKEW LGNFVPGTYL DHGTKAITYT
DFVNKELILF SIADNMRSIP SIADGLKPGQ RKVLFSCFKK NVTKDKKVVE LAGYISEQSA
YHHGEQSLQQ TIIGLAQTFV GSNNINLLEP SGNFGSRLAG GSDAASPRYI STRLSPFARK
IYLAEDEPNL KQQYDDSNVI EPEVYTPIIP MILVNGADGI GTGWSTSIPN YHPTDIVKNL
KRRMGRLNLA EEEELPFEPM MPWFRGWKGT PEAAGPDRYK FNGIAYQNDQ NPNEVVITEL
PIRVWTDDFK TKLEKIISGT EGPAWIKDYK EFNDHNTVHF EIMLDEKFMP KVLEEGLLER
FKLQKQVATS NLVAFDMQGR IRKYDKVEDI MEEFYHYRLD MYSERKKYWL NVYHRDYRKL
KNQARFVQEI ISGVLVVGKK KKQALITELR ERKYEGFPPN KAGAKAEEEE LGNTSDADDD
SSGALDAGSK DYDYLLSMAI WSLTAERLQK LLDAIAKKKA EHDELQAKSE KDLWCEDLDA
LMAEWDKQVA IDAEIQTKIR RLGRRVSKKI GAGKNRKAKD EDEYEPEKKS RAKGKAAVAK
PKVETKTAQR FADMFSSKPK VKKENDADVV ELFDDFSDDD FAALSRKPAA SKRTKAVPAT
ASASQSQSEE PEARPVKRAA ASKARALFDA DSASENEDDD VVDVDSLVKG IGAPKKSASP
APLSKSISAR SFQIDDDDDD VLASSAPAKP MTKEDILDSL LSDEDKPSTS NISGYAALKK
IARPKAVAAK AKPKAAAKPK AASKQTTLSP AAKAYAARKA SALADDSDED VAAPGSPSPK
RAPARARPGR AAAARRPIVV DEDDSLLADD QDESDDPFEM DDDDD
//
