ID A1DP90_NEOFI Unreviewed; 1735 AA.
AC A1DP90;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 113.
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=NFIA_059660 {ECO:0000313|EMBL:EAW16611.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW16611.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR EMBL; DS027698; EAW16611.1; -; Genomic_DNA.
DR RefSeq; XP_001258508.1; XM_001258507.1.
DR STRING; 331117.A1DP90; -.
DR EnsemblFungi; EAW16611; EAW16611; NFIA_059660.
DR GeneID; 4585024; -.
DR KEGG; nfi:NFIA_059660; -.
DR VEuPathDB; FungiDB:NFIA_059660; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_1_1_1; -.
DR OMA; TWTQDFK; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000006702; 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:UP000006702};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 554..668
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1119..1146
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1297..1325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1500..1537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1681..1697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1716..1735
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1735 AA; 193347 MW; 7A9CD62DAD20D97D CRC64;
MDDSIMEGSV FEDDGSSDFV PEPAAKPKAK AAPKKAAPKK MTQTKLTAKP AAKATASKKR
SKPDSEDDLS DDMGMSDDDS SLSQTPPKKV KKAPASKKGG SKPLADVENE SFGGDVGDQP
AKSTNASEKY QKLTQLEHII KRPDTYIGSV ERTTQFMWVY DSEMEGMKYR EVSYVPGLYK
IFDEIVVNAA DNKQNDANMD EIRVTIDRES GEISVWNNGR GIPIEIHAKE GIYVPELIFG
HLLTSSNYDD TQQKVTGGRN GFGAKLCNVF STEFTIETQD SRQKKKYKQT WTNNMSKMGK
AKITDAKGDD YTKVTFKPDY AKFGMEGMDD DFEALVKRRV YDLAGTAKVA VKLNGSRIPV
RNFKKYMEMY TKAIRRERGE EDTNAKDEII TCSPDPHWEI GFTVSDGSFH QVSFVNSIAT
TSGGTHVNYI ADQICARLAD QVKKKNKNGA TLKPAQIRNH IFIFVNALIV NPAFTSQTKE
QLTTKSSQFG SKCTLEEDFY KKILKTEVMN NILHFAQAKA DQLLKKTDGG RRTRMNNPKL
VDANKAGTKD GHHCTLILTE GDSAKGLAMA GRAVVGPDLF GVFPLRGKLL NVRDASFEQI
SKNQEIQNIK NFLGLQHKKE YTDTRGLRYG HLMIMTDQDH DGSHIKGLLI NFLQAQFPSL
LKIPEFLIEF ITPIVKVWKG DPKNPTKQRS FFTMPEYEAW KEEHKHERGW EHKYYKGLGT
STTEDAQVYF RDLDRHLKEF HTMQDHETEL IELAFSKKKA DERKEWLRQF KPGTFLDHSV
EKITYTDFIN KELILFSMAD NQRSIPSVVD GLKPGQRKVL YTCFRRNLKK DMKVVELAGH
VSGMTAYQHG DASLQQTIVG LAQTFVGSNN INCLEPSGNF GSRLQGGQDC ASARYIYTRL
SPFARRMFHA ADDPLLTYNE DDGKKIEPEV YVPVVPLILI NGADGIGTGW SSSIPNYNPE
DIVDNLKRLM DSQPVKPMQP WFRGFTGEVT ALGGDRFKFS GIIKETGDKE VEITELPIRT
WTQDFKDKLE EIIKAEKTPS FIKDYKDYNT HTKVHFVIQM DEKNIKSAVA EGLEEKFKLS
KTIATTNLVA FDPEGRITKY ASVDDILKEF YAVRLKFYER RKQYQLSELQ KELDKLTNQA
RFVQMIIDGD LVISKKKKPV LVAELKKHGF KAFPKVIDAV KAGEDAPVVE EEEDESGNDE
TEVLSSAYDY LLGMPLWSLT HERVEKLRRQ IGEKEVEMDA LIKLSKEDIW KRDLDDFINE
WRFQLEDEAR RQRKVANMGR RTSAKLMTAA GRGKATKKRK AALDDDSDDE DFAAPKTKKS
AAAKKTEPKG GLLSYLGKPS AKPAPASAPS GDGGDSDDDF EVEVLPKKNR GAATKAATKV
KDEDEVMDDL GEEILPKKSR GPAKPAPKPK EEDDGDSEDI APKKGRAAAK AKPKPKDEDD
DELDDDEFME IAKAEAAKSA KSQPTRTSRK ITNYTALDDS DSDNGDDLLG DVSKMVKGIG
GTTGDSTTDS RQLFSERSRP SSSSSGLKVS SSKPSKLSTD FDADETDYSK LIPQNSPRRS
LQVKPKETKV NDDFDMDDDD DEEPVKPAAK AKPVAKGKSA TTAAASKPAA APKPRGRPKK
DAPKPAAPAP SLKQTTLSPA AKAYASKQAK ATATKKKQLV DDLSDDDIDA MANDILDSPA
GKMDVSEDDE PPKRKTTARP ARRTAAAKKT YVIEDDSEDD DGGDSGDDFD EEDSD
//
