ID A0A364NH39_9PLEO Unreviewed; 1713 AA.
AC A0A364NH39;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=DDE83_000148 {ECO:0000313|EMBL:RAR16580.1};
OS Stemphylium lycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Stemphylium.
OX NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR16580.1, ECO:0000313|Proteomes:UP000249619};
RN [1] {ECO:0000313|Proteomes:UP000249619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL Submitted (MAY-2018) 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:RAR16580.1}.
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DR EMBL; QGDH01000002; RAR16580.1; -; Genomic_DNA.
DR STRING; 183478.A0A364NH39; -.
DR Proteomes; UP000249619; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 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; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362094};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362094};
KW Hydrolase {ECO:0000313|EMBL:RAR16580.1};
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|RuleBase:RU362094};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000249619};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 569..685
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1642..1663
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1697..1713
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1713 AA; 189057 MW; 993EF8DBDC3701E3 CRC64;
MDDSLMEDSV FDEGASSDFA PPAKPAKATK AAAKPKAAAP KKAAGPAKPR GRPAGAAAKP
KAAPKKKAKA DSDVDENSDM DLDDAPVDND ESLLADTPPK AKKAVAPKKS SGKPLADVAN
ESFGADGDDA PAAKPKKGGA SSKYQMLTHL EHIMKRPDTY IGSVERQTNS MWVFNTESES
MEFREVSYVP GLYKIFDEIL VNAADNKQND KNMSEIRVTV DRETGEISVK NDGKGIPIEI
HKEHGIYVPE MIFGHLLTSS NYDDDQQKVT GGRNGYGAKL CNVFSTEFTV ETVDSKQKKK
YKQTWTENMS KMGKAKITDI KTDDYTKVSW KADYARFGME GIDDDFEAMV KRRTYDMAGT
LRGVKVYLNG DRIKIGTFAK YMEMYTKSIS RDQGRSEDDK EKDVIITDKL DRWDVGFAVS
DGSFNQVSFV NSIATTSGGT HVNLIADQII DKLMAIVNKK NKAAVKLKPA QIKNHLFLFV
NCSIVNPAFT SQTKEQLTTK ASQFGSKPVL SDKFLNAIAK TDVIQNIMHF AQQKADQMMK
KTDGNKRNRI SNAKLTDANK AGTKDGHLCT LILTEGESAS VLALAGRAVV NQDLFGVFPL
RGKLLNVRDA TVDQIMKNAE IQNIKKFMGL QHKKEYTSAD MKSLRYGHLM IMTDQDHDGS
HIKGLLINFL QCQFPSLLKV PGFLLEFITP IVKVWKGDPK NPRGMKSFFS MPEYEEWKEQ
HAHEKGWDHK YYKGLGTSDI PDAQIYFKDL DTHMKRFQVM RAEEEKLIEL AFSKKKADAR
KDWLRDFVPG QHLDLTTPDI SYDDFVNKEL ILFSMADNVR SIPSVIDGLK PGQRKVLYTC
FRRNIKKDVK VVELAGSVSG STDYAHGEAS MQGTIVGLAQ NFVGTNNINY LEPSGNFGSR
LKGGADAASA RYIYTRLSPF ARRIFHAHDD ALLQYGESDG HKIEPEMFVP ILPTILINGS
SGIGTGWSSE IPNFNPMDII ENIKRRMQPG ATKEDMTPMI PWYKGFTGST TVLGPDRYQF
TGTVRQTGDN EIEITELPVR YWTQDFKEKL EEIIKAEKTP SFIKDYIDYN TPDRVHFVIK
MEDKYMATAL AKGLEEMFKL FKPQATSNLV AFDAHGRIHK YAGVLDIIEE FYHVRLRYYE
KRKQHQLQVM EKEHLKMSNQ ARFIQMIIDG KLTISKKKKA VLVQELKKHG FTPFPKVEEA
KDAGEVEDAQ EDESDDNEVE VSANDYDYLL GMAIWSLTQE RVEKLLKQLG EKQEEIDTLI
KLSPKDIWTV DLEAFMDEWN LQLEEEAKRK KKIAGITRRA SQKLGIGAGK GGKGKKKRKM
DGSDSDDSAS DFGPVKKKAK PKKEGLLSYL QQEPTKKPSA AEALKSSSAF GSAAPQKQGT
LLSHLVKKEG TPQTDGASES RPDSEDSKPA PSKRGRPAAA KAVKKDPVLS DDEDSDVFAA
VAQEAAKEPT KTEIPSRGGR AATKQAPKYS LGSDSDDDDD DLLGDVSSMV KTIGAGSNGV
PMFKATTAAR PGSNGRARSG SAAGAKKGSP IDIDGDTTNY EGLMPQPSPK RPAPRNVNDT
IMSSDDDDFD LSVKKPAASK LTAKPAAKPK AAAAKPAPKP KAVAKKPAAQ SPAAKAYAKK
HGKDAAPAKP AAKKKQITVD SDEEEDMDDA EDIANDILSD EDEDEPTPKP ASRAPAARPG
RRAAAKPAKY VVSDDEAESD EASEPSFDDD ESE
//