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Database: UniProt
Entry: A0A364NH39_9PLEO
LinkDB: A0A364NH39_9PLEO
Original site: A0A364NH39_9PLEO 
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
//
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