ID M2ZV72_PSEFD Unreviewed; 1278 AA.
AC M2ZV72;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=MYCFIDRAFT_164213 {ECO:0000313|EMBL:EME82904.1};
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855 {ECO:0000313|EMBL:EME82904.1, ECO:0000313|Proteomes:UP000016932};
RN [1] {ECO:0000313|EMBL:EME82904.1, ECO:0000313|Proteomes:UP000016932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86 {ECO:0000313|EMBL:EME82904.1,
RC ECO:0000313|Proteomes:UP000016932};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB446558; EME82904.1; -; Genomic_DNA.
DR RefSeq; XP_007926289.1; XM_007928098.1.
DR AlphaFoldDB; M2ZV72; -.
DR STRING; 383855.M2ZV72; -.
DR GeneID; 19332159; -.
DR KEGG; pfj:MYCFIDRAFT_164213; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_1_0_1; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000016932; 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; 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|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:UP000016932};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 442..556
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1166..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1278 AA; 146088 MW; 48B13E5B97FB88D9 CRC64;
MDVPVEQKAK KGSEQYEKLT QLEHILKRPD TYIGSVEQTT EQMWVYNSET ESMENRKVTF
VPGLYKIFDE ILVNAADNKQ RDKNMNELRV WVDAEKGVIS VKNNGKGIPI EMHTKEGIWI
PEMIFGHLLT SSNYDDNEAK TTGGRNGYGA KLTNIYSTQF ELDTVDSKSK QRYRQTWRKN
MSVMEKAKID KVKVDDYTQV TFRPDFSKFG MEKMDADFEA LVKRRVYDMA GTAKGVKVYL
NGERIKISKF KQYMEMYTKA IKTENIVNDG TAPEQVILTD NPHERWEIGF AVSDGSFQQV
SFVNSIATTS GGTHVNYIAD QICDKLEEIV NKKNKGGVKL KKAQLKNHIF LFVNALIVNP
AFTSQTKEQL TTKVSAFGSR PQVSEKFLKD IAKTEVVNNI LHFAQQKADK VLAKSDGGRR
QRMNHSKLTD ANKAGTKDGH RCTLVLTEGD SAALLALAGR AVVNPDLFGV FPLRGKVLNV
RDASVDQISK NQEIQNIKKF IGLQHKKEYT DTRGLRYGHI MIMTDQDHDG SHIKGLLINF
LQVQFPSLLK IPGFLLEFIT PIVKVWKGDP KHPKAKHDFF TMPEYEAWRE QPGHSKGWDH
KYYKGLGTSD TRDAQIYFAD LDKHLKTFHA MQDHEPELLE MAFSKKKADA RKTWLQNFVP
GTYLDMSGTE EITYDDFINK ELILFSMADN QRSIPSVIDG LKPGQRKVMY TCFRRNMKKD
MKVVELAGLV SGLTAYPYGD ASLQQTIVAM AQNFVGSNNM NVLEPSGNFG SRLQGGSDAA
SARYIYTRLS PFARKIFHQS DEALLTYNLD DGKTIEPEQY VPILPMVLIN GAEGIGTGWS
TSIPQYKPDD VIDNLIRRMD VGEKDAMQPM TPWYRGWTGQ TDQIDDTRFK FTGKIEVIDE
TTVRVTELPV HYWTQAFKDK LEDIIKAEKT PSFIKDYVEY NTPETVHFEI KLEAKTLQQN
EGKLEELFKL SNTQVTTNLV AFDPQGRIYK YASPLDIIEE FYHVRLQKYQ QRKDWLLSEM
HKELDKLNNQ ARFVNMIIKN ELVVSKKKKA VLVKELDKLG FTRFPKVIEA KKQGELEEVV
EDDNEESDDA EVAAGANDFD YLLGMPIWSL TEERVAKLNK QIGDKEVEID ILTAKSPQDL
WKEDLTELRT EYQAYLDEEK ARDKKINANG RRASGKLGIG GQASKKRNAN DSDASESDFA
PRSQRRPNLR LLMDCSAWAP RLSRSQQVST QLLMALSRNL LHRHQPRSRS LWRMRSSRRD
LSPSLPGLHR RLPQIRKR
//
