ID K3VTY4_FUSPC Unreviewed; 1652 AA.
AC K3VTY4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=FPSE_00841 {ECO:0000313|EMBL:EKJ78984.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ78984.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ78984.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ78984.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
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:EKJ78984.1}.
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DR EMBL; AFNW01000016; EKJ78984.1; -; Genomic_DNA.
DR RefSeq; XP_009252236.1; XM_009253961.1.
DR EnsemblFungi; EKJ78984; EKJ78984; FPSE_00841.
DR GeneID; 20359461; -.
DR KEGG; fpu:FPSE_00841; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_2_0_1; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000007978; Chromosome 4.
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; 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:UP000007978};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 535..649
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1212..1239
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 75..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1652
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1652 AA; 184910 MW; B86FA293FA9B196F CRC64;
MDSDESMFSL EDESDGFVPE TKAKPKKAAA PKKPAAPKKM VQSTLKTKAQ PKKRPTPESD
NDDASVASDA SNTPPKAKKQ KKEADDDSMA IDSPAKPAKQ KTATEMYTKL TQLQHILKRP
DTYIGSVERT EQQLWVLNKE TQLMEYKAIN FVPGLYKIFD EILVNAADNK QRDSSMTYMK
INIDREAGVI SVENNGKGIP IVLHEKENIY IPELIFGHLL AGSNFDDDEK KTVGGRNGYG
AKLCNVFSTE FNLECQDSVS GKKYKQTWTD NMNTMHKAKI TASKSASYTR ITFKPDFKRF
GMEDGIDDDL ESLMYRRVYD MVGTIRGIKV FLNGEQVKIK DFKAYCDLYA KSIAKDRLDE
EGGSPICTVE MDKDKSHPRW EVGFAVSDGT FQQVSFVNSI ATTAGGTHVN YIADQITKSL
LNTLNKKRKG HTLKQNHLRN HIFVFINCYI DNPAFSSQTK EQMTTKASQF GSKCALGDEF
LKKVAKSDAI QNILDMAEKK ADKMMAKSDG NKRSRVNNAK LVEANFAGTR RGHECTLILT
EGDSAKGLAV SGRAILDPDR IGVFPLRGKL LNVRDASPDQ IAKNQEIQNI KQFLGLKHKT
SYTDTKNLRY GHLMIMADQD HDGSHIKGLL INFLEVQFPS LLRIPDFFRE FITPIVKVWQ
GPNPKKPQKL KSFFTQPEYE EWKDVHKNEL TRWHSKYFKG LGTSSNEDAQ VYFTNLDDHL
KEFEVMKPEE SKMLELAFSK KKADARKEWL GNFVPGTFLD HSAKQICYSD FINRELILFS
MADNMRSIPS VLDGFKPGQR KVIYACFKRN LIKDKKVVEL AGYVSEQTAY HHGEQSLQQT
IIGLAQNFVG SNNINCLEPS GNFGSRLAGG SDAASPRYTF TRLSPFARKI FHPMDEPNLL
HHYEDGKKIE PMVYAPILPM VLVNGADGIG TGWSSNIPNY HPADIVHNLR RRMGRLDEND
TEEKPFETMM PWFRGWKGTP EAAGPDRYKF NGVAYANEQK DNEIVITELP IRVWTDDFKA
KLEKVISGEL GPSWIKDYKE FNDHSTVHFE IAVDDKHMGK VMEEGILERF KLTKQVATSN
LVAFDTSGRI RKYEKVEEIL EEFYQYRLDM YTDRKKHWLG VYHADLRKLQ NQARFIKEII
DNKLVVGKKK KAVLVQELRD RDYEAFPPRG DKKKTADEEE EDEDNQEVEG DSEGGARDYD
YLLSMPIWSL TAERLEKLKQ AIEKKKAEHE ELLALSEKDL WCRDLDDFMT EWENQLAVDA
EIKTNIRRLG RRVSKKIGAG TARGRKAKDD DEYAPEKKAR AKAKAAVVKP VKVETKSAQR
FAEMFSSKPK VKKEPTADVM ELSDAFSDDD YAALSRGKSS APAMKASQSP PTETPGTGRA
KRAAASKIKA VIDDDDSESD DDQMLGDVGA LVKGIDKPAG DHEKGRFSLH AMSRPDSSHG
NTSNSGLPKA KAKSAKAFDF DDDSPDDTNY ELLAKSSPHK TAAKDDHVDS FLSDDEPFVA
PAKPTSAKSK STGTESEDPT PAGLATVKKG RGRPAGAKSK EAAKPKAAPK AATKVTKTAA
SKVASRPATK QTTLSPAAKA YAAKKAVKKP VLDDDSDEDM ADPESPPPKA AARARPGRAA
AARRPIVVDD DDSSIEQPDE SDDPFSMDDD ED
//
