ID A0A420HJ60_9PEZI Unreviewed; 1733 AA.
AC A0A420HJ60;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=GcM3_188004 {ECO:0000313|EMBL:RKF57463.1};
OS Golovinomyces cichoracearum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Golovinomyces.
OX NCBI_TaxID=62708 {ECO:0000313|EMBL:RKF57463.1, ECO:0000313|Proteomes:UP000283383};
RN [1] {ECO:0000313|EMBL:RKF57463.1, ECO:0000313|Proteomes:UP000283383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG3 {ECO:0000313|EMBL:RKF57463.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
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:RKF57463.1}.
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DR EMBL; MCBQ01018810; RKF57463.1; -; Genomic_DNA.
DR STRING; 62708.A0A420HJ60; -.
DR Proteomes; UP000283383; 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:UP000283383};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 569..686
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 24..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1711..1733
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1733 AA; 196372 MW; 8A281D99191A5CFF CRC64;
MEDSLLEISD DSEDFMPQVK PKAKLVVKKP AAQKVSRPAK ISKAPPKKLI QTSIQSTKSN
VKKRPKLDSD EDEITSLAID SVSYDSAPPD SPPNAKKQKN TDTAKHGLGK TSPDFDDSDS
NHGQSPEPKP KPPKKKDATD QYQKLTQLEH IVKRPDTYIG SVERTEQMMW VFNSELQRME
FRKVRFVPGL YKIFDEILVN AADHKQVDPS MKQIKVTIDR EKGEICVEND GRGIPVEIHK
KEKVYIPEMI FGHLLTGSNY DDDEQKTTGG RNGYGAKLCN IFSTQFTLET QDSENVKRYK
QVWTENMTKM SKAKITTSKT SDFTRITFTP DYKRFKMDGI DDDFEALMKR RVYDLAGTVK
KVKVFLNGAL IKLDFKKYME MYARAINLER GMEPSENDKV SVIVENSETH EKWEVGFAVS
DGSFQQVSFV NSIATTSGGT HVNYIADQIC EKLMDVVKRK NSKGAVLKTN QIRNHIFLFV
NCLIVNPAFT SQTKEQLTTR PKQFGSKCIL SDKFLKEIAK TDAVQNIINF AQAKADQVLA
KSDGNKRSRM SNAKLVDANL AGTKRGHECT LILTEGDSAK GLAVAGRAIL DPDRIGVFPL
RGKLLNVRDA SIDQISKNAE IQNIKQFLGL KHKQVYNETS GLRYGHLMIM ADQDYDGSHI
KGLLINFLQV QFPSLLKISD FFREFITPIV KVWKGPNPKK PISQKSFFTL PEFEEWRERH
NNDKGWKHKY YKGLGTSLPE DAQVYFSNLD DHLREFETMK PEEEDLIELA FSKKKADARK
HWLGNFVPGT FLDHSTKTLT YDDFVNRELI LFSMADNLRS IPSVIDGFKP GQRKVMYACF
KRNLVRDMKV VELAGYVSEN TAYHHGEASM HQTIIGLAQN FVGSNNINCL EPSGNFGSRL
TGGIDAASPR YIFTRLSPFA RRVFSAQDEP LYEHNVDDGR SVEPTMYCPV VPMILVNGAD
GIGTGWSTTI PNYNPIDIVN NLKRRMGRLD DSKEEKPFET MKPWFLGWKG ISEEAGPMRY
NFTGLIRMVG ANEVEITELP IRMWTDDFKT KLEEIIKGEK APSFIKDYKE YNDHKRVHFI
IQLDEKNADE RIKNNLVEKF KLQKSIATSN LVAFDTRGKI RRYEKVEDIL EEYYVYRFEM
YTKRKAYWLE QINFEKRKLE NQARFVLEII DNKLVVSRKK KSVLVAELRQ RNYEPFPKFK
DPQKSTEADD SADNEDEEDS NNHDDAQDYD YLLRLPIWSL TQERVDKLKN QILNKTKEFN
DLQNLSEKDL WCKDLDDFVQ EWNYQLREED EYQKKIHNTN RRASRKIGAG GKGANNRAKR
PKEDEDFNPS SRKANNTKGA QLKTQQNLIQ SFTKSNKVSE SVMEPKKESQ ALKKPKNEPQ
GLTKVKKETE ELTAPLSDDE FEAGALLASN FASQKPSKPQ KKSDTSNGRK KRAVAPKIYK
LESDEDSNNS SLDLLDDIGD LGSMVKGIGS QNDTGTGPSN GRMSLFQSRP SISQGSGSIL
PKLKTKPSRG FDDDDGEDDT NYEMLARSSP HKPAASKENI DSFLSDDDLM PFTKTVPLKS
VAKSTAMFKK SVSSTKNGES KKKNSTGSSG ETENIAKVRK SRLKAMDKFS DDDEVEINDS
PPPKPISRIN SKPLAKGWKS DKNQNINDSG NELASSKPGS VKLASGMKLM GDTISDDEDE
SIVQRGIGRS RPARAAAKKK STKPVYVSSE NEETAEDETE ESENTGNDYS ESE
//
