ID A1CUL0_ASPCL Unreviewed; 1735 AA.
AC A1CUL0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 109.
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=ACLA_087000 {ECO:0000313|EMBL:EAW06997.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW06997.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW06997.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS027060; EAW06997.1; -; Genomic_DNA.
DR RefSeq; XP_001268423.1; XM_001268422.1.
DR STRING; 344612.A1CUL0; -.
DR EnsemblFungi; EAW06997; EAW06997; ACLA_087000.
DR GeneID; 4699965; -.
DR KEGG; act:ACLA_087000; -.
DR VEuPathDB; FungiDB:ACLA_087000; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_2_1_1; -.
DR OMA; TWTQDFK; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000006701; 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:UP000006701};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 554..668
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1119..1146
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1297..1324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1500..1534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1735 AA; 192749 MW; EC54155510E365AD CRC64;
MDDSLMDDSM FDSEGSSDFV PEPAPKPKAK AAPKKAAPKK LTQTKLGAKP AAKATASKKR
AKPDSEDDLS DGMGMSDDDA SLAQTPPKKV KKAPAAKKGG SKPLADVENE SFGGDAGDEP
AKSTNASEKY QKLTQLEHII KRPDTYIGSV ERTTQHMWVY SSTTEGMEYR EVSYVPGLYK
IFDEIVVNAA DNKQNDAKMD EIRVTVDRES GEISVWNNGR GIPIEIHSKE GIYVPELIFG
HLLTSSNYDD TQQKVTGGRN GFGAKLCNVF STEFTIETQD SRQKKKYKQT WTSNMSKMGK
AKITDAKGDD YTKVTFKPDY ARFGMDGMDD DFEALVKRRV YDLAGTAKVA VKLNGSRVPI
RNFKKYMEMY TKAIRRERGE EDAGAKDEII TCSPDPHWEV GFTVSDGSFH QVSFVNSIAT
TSGGTHVNYI ADQICVKLAD QVKKKNKNGA TLKPAQIRNH IFIFVNALIV NPAFTSQTKE
QLTTKSSQFG SKCVLEEDFY KKILKTEVMN NILHFAQAKA DQMLKKTDGG RRTRMNNPKL
VDANKAGTKD GHHCTLILTE GDSAKGLAMA GRAVVGPDLF GVFPLRGKLL NVRDASFEQI
SKNQEIQNIK NFMGLQHKKE YIDTRGLRYG HLMIMTDQDH DGSHIKGLLI NFLQAQFPSL
LKIPEFLIEF ITPIIKVWKG DPKNPTKQRS FFTMPEYEAW KEQHGHERGW EHKYYKGLGT
STTEDAQVYF RDLDRHLKEF HTLQDHETEL IELAFSKKKA DERKEWLRQF KPGTFLDHSV
AKITYTDFIN KELILFSMAD NQRSIPSVID GLKPGQRKVL YVSFRRNLKK DMKVVELAGH
VSGMTAYQHG DASLQQTIVG LAQTFVGSNN VNCLEPSGNF GSRLQGGQDC ASARYIYTRL
SPFARRMFHP ADEPLLTYNV DDGKQIEPEN YVPVVPLLLI NGADGIGTGW SSSIPNYNPE
DIVDNLKRLM DGEPIKPMQP WFRGFNGEVT AIGGDRFKFS GIIKEAGDKE VEITELPIRT
WTQDFKDKLE EIIKADKTPS FIKDYKDYNT HTKVRFVIQM DEKHMQSALS EGLEEKFKLS
KTIATTNLVA FDPEGRITKY ASVDDILKEF FTVRLKFYER RKQYQLSELQ RELDKLSNQA
RFVQMIIDGA LVISKKKKPV LIAELKEKGF KAIPKVADAV KAGEDEPVVE EGEESEEAED
TEVQSNAYDY LLGMSLWSLT QERVEKLRRQ IGEREVEIDA LIKLSKEDIW KHDLDVFINE
WRFQLEDEAR RERKVANMDR RRSAKLMTAG GRGPAKKRKA ALGDDPDDED FAAPKSKKTT
AAKKSEPKGG LLSILGKPSA KPAAAPSGDG DGSDDDFEVE VLPKKSRGAA KAAPKVKDED
DEMDIEVLPK KSRAPAKPSP QPKDEDEEGS DVEIVPKKGR AAAKPKAKPK DEDEDDLDDD
DDDFMEIAKA EAAKSAKSQP ARASRKPATK YTVSDDSDSD NGDDLLGDVS MMVKGIGGTA
GDTTSDSRQL FSERSRPGSG SSALKASSSR LSKLSTDFDA DETDYSKLIP QNSPRRSLQV
KSKEVKTSDD NDLEDEVEDE DDEPVKPAAK AKPAAKAKPA TKAKSATTAA ASKAAAAPKP
RGRPKKDAAK PAAAASSLKQ TTLSPAAKAY ASKQAKATAT KKKQLVDDLS DDDIDAMAND
ILDSPVGKMD VSEEDEPPKR KAAARPARRT TTKKTYVIED DSEDGDSGDD FDESD
//
