ID A0A010QMY1_9PEZI Unreviewed; 1774 AA.
AC A0A010QMY1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=CFIO01_07750 {ECO:0000313|EMBL:EXF78070.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF78070.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF78070.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF78070.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) 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:EXF78070.1}.
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DR EMBL; JARH01000666; EXF78070.1; -; Genomic_DNA.
DR RefSeq; XP_007598293.1; XM_007598231.1.
DR STRING; 1445577.A0A010QMY1; -.
DR KEGG; cfj:CFIO01_07750; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_2_0_1; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000020467; 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:UP000020467};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 543..661
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1575..1774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1205
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1401..1423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1586..1609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1666..1680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1756..1774
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1774 AA; 198080 MW; A7C49CAFDD978ECB CRC64;
MSSDEASVFS MGEESDFAPA KPKAKAAAVK KAPAKKLTQT TLKTKAVPKK RAKPESDDED
GASTFSNTPP SAKKLKKAPA AKKSSGNPLS EIENDSMMID DEEPAAPKTK KNATDTYQKL
TQLEHIIKRP DTYIGSVEPT EQPMWVFNKE TKLMEYRKVT FVPGLYKIFD EILVNAADNK
QRDATMTTMK ITVDREAGEI SVENNGKGIP VEIHGKEKIY IPEMIFGHLL TGSNYDDDEK
KTVGGRNGYG AKLCNVFSEQ FTLECQDSNN GKRYKQVWTD NMSKCGKAKI SSSKTSDFVR
VTFKPDFKRF SMTGIDDDLE ALINRRVYDM AGTVRGIKVY LNGTHIKLAF KGYCEMYAKA
ISKERGAEEG VEPKVVVEVD KTDAHPRWEI AFTVSDGSFQ QVSFVNSIAT TSGGTHVNYV
ADQITGSLLK TLDKKKKGHA LKQNHIRNHI FIFVNCLVNN PAFTSQTKEQ MTTKVSQFGS
KCPLTEEFLK KIAKSDAIQN IIDFAEKKAD KMMAKSDGNK RSRISNAKLV DANLAGTRHG
HECTLILTEG DSAKSLAVAG RAILDPDRIG VFPLRGKMLN VRDASIDQIT KNAEIQNIKQ
FMGLKHKQTY TDTKSLRYGH LMIMADQDHD GSHIKGLLIN FLQVQYPSLL QIPDFFREFI
TPIVKVWQGP NPKKPQRLKS FFTQPQYEEW KDSNRNDLSR WHYKYFKGLG TSSNEDAQVY
FTNLDDHLKE FDTMKTEEAD LFDLAFSKKK ADARKEWLGS FVPGTFLDQS TKTISYTDFV
NKELILFSMA DNMRSIPSVL DGLKPGQRKV MYACFKRNLV KDQKVVELAG YISEQTSYHH
GEVSLQQTII GLAQTFVGSN NINCLEPSGN FGSRLAGGSD AASPRYIHTR LSPFARKIFS
PLDEPNLDSQ YEDGKRIEPK VYAPIIPMIL CNGADGIGTG WSTSIPNYHP IDIVNNLKRR
MGRLDGEDGE DGVFQTMMPW FRGWKGTPEQ AEKDRYKFNG ICELDEKTGE VIITELPIRM
WTDDFKAKLE EVISGTKGPV WIKDYKEFND HKNVHFVIQM DDKQVKDVMK DGLMERFKLS
KQVATSNLVA FDTNGQIRKY EKVEDILEEF YHYRLDMYAQ RKKHWLGVYH SDFRKLSEQA
RFIREIIDGK LVVAKKKKQV LVEELAKRKY EPFPRNKDKN VKKKSTDEDM EGNDDGEEEE
TDEQTNGYDY LLSMPIWNLT YERLERLQKQ IENKKAEHDA LLALSEKDLW SKDLDEFVAE
WETQMAMDAE IQTNIRRLGR RVSKKIGAGK GRKTKKEDDD YAPGEKKRPG PKAKAAAKVT
EKAADRFAAM FEKDKTKPKK EDADSDAFSD NDFAALGGRK NAAKPAAEPT RPRAAATKKK
PVYQLSDTDD DDEDFASLGK STSAPAESAV EDDNSSQSQK SAAAKKPAPK KSAVKEPSPK
VEELLSDDDD DFENLGSKRT SSDKAASKSA SVEPAPKSKR AAATKKYIIE DESDEDDDDF
QSAAEMSASP EPKPAKPAAN GRNQRAATAT KKSKYVIDDE SEESEVEENH IGDIGSLVRG
IGAPKSETEK GRLSLFAMNR PDNGRDSTLP KIKTKASRTF DDDSVDDTNY EMLARSSPHK
TFNKGDDIDS FLSDDGAPAT KGSKAKDTKA APAAAVAKKA RGRPAGAKNK AKDAEAAPAP
KAKPKAKAAP KPPTLSPAAK AYAAKKATKR VVSDDDEDDV DMEDPESPPR PAARSRPGRA
AATKAKAKPT YVIEDDSEMD VDQSEDPFDM DESD
//
