ID B2VZ36_PYRTR Unreviewed; 1722 AA.
AC B2VZ36;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
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=PTRG_02676 {ECO:0000313|EMBL:EDU45199.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU45199.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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; DS231616; EDU45199.1; -; Genomic_DNA.
DR RefSeq; XP_001933009.1; XM_001932974.1.
DR STRING; 426418.B2VZ36; -.
DR EnsemblFungi; EDU45199; EDU45199; PTRG_02676.
DR GeneID; 6340899; -.
DR eggNOG; KOG0355; Eukaryota.
DR HOGENOM; CLU_001935_2_0_1; -.
DR InParanoid; B2VZ36; -.
DR OMA; TWTQDFK; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000001471; 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; 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; 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:UP000001471};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 569..685
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1502..1722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1502..1530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1644..1670
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1706..1722
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1722 AA; 191002 MW; FCD1AD53F1214362 CRC64;
MSDMEDSIFD EGASSDFAPP AKPAKAAKVA KPKAAAPKKA AGTAKPRGRP AGATAKPKAK
AAPKKKKADD SDMDENSDID MDEDPVDDDE SLLKDTPPKA KKAPGPKKSS GKPLADIPNE
SFGGDDDDDV PISKPKKGGA SSKYQMLTHL EHIMKRPDTY IGSVERQTDK MWVYNSESDS
MEFRDVTYVP GLYKIFDEIL VNAADNKQND KNMSEIRVTV DRETGEISIK NDGKGIPIEI
HKEHGIYVPE MIFGHLLTSS NYDDDQQKVT GGRNGYGAKL CNVFSTEFTV ETVDSKQKKK
YRQTWTENMS KMGKAKISDI KSDDYTKVSW KADYARFGMT GIDDDFEAMV KRRTYDMAGT
LRGVKVYLNG DRIKLTSFAK YMEMYTKSIS RDQGKSEDDK EKDVIITDKL DRWDIGFAVS
DGSFNQVSFV NSIATTSGGT HVNHIADQIV EKLMAIVNKK NKAAVKLKPA QIKNHLFLFV
NCSIVNPAFT SQTKEQLTTR PSQFGSKPVL SDKFLNAIAK TDVIQNIMHF AQQKADQMMK
KTDGNKRNRI SNAKLTDANK AGTKDGHLCT LILTEGESAS VLALAGRAVV NQDLFGVFPL
RGKLLNVRDA TVDQIMKNAE IQNIKKFMGL QHKKEYTMAD MKSLRYGHLM IMTDQDHDGS
HIKGLLINFL QCQFPSLLKI PGFLLEFITP IVKVWKGDPK NPRNMKSFFS MPEYEEWKEQ
HQHEKGWDHK YYKGLGTSDI PDAQIYFKDL DTHMKRFQVM REEEEKLIEL AFSKKKADAR
KDWLRDFVPG QHLDLTTPDI SYDDFVNKEL ILFSMADNVR SIPSVIDGLK PGQRKVLYTC
FRRNIKKDVK VVELAGSVSG STDYAHGEAS MQGTIVNLAQ NFVGTNNINY LEPSGNFGSR
LKGGADAASA RYIYTRLSPF ARRIFHGHDD ALLKYGESDG HKIEPEMFVP ILPTILINGS
SGIGTGWSSE IPNFNPMDII ANIRRRMEPG ATKDDMTPMI PWYKGFTGTT TEIGPDRYQF
TGTVRQTGDN EVEITELPVR YWTQDFKEKL EEIIKAEKAP SYIKDYIDYN TPDRVHFIIK
MEDKYMAEAV TKGLEEYFKL FKPQSTSNLV AFDAHGRIHK YATVLDIIEE FYHIRLRYYE
KRKQHQLQVM EKEHLKMTNQ AKFIQMIIDG KLTVSKKKKA VLVQELKKLG FTPFPKVEEA
KQAGEVEDYQ EDEASEDADV EVSANDYDYL LGMAIWSLTQ ERVEKLMKQI GEKQHEIDTL
IKLSPKDIWN VDLDAFMDEW NLQLEEEAKR KKKIAGITRR ASQKLGIAAG KSSKGKKKRK
MDGSDSDDSG SDFGPVKKKA KPKKEGLLGY LQSEPAKKPS AAEALKSSSA FGSTALQKQG
TLLTHLVKKK EEPPQVDGAA ESRSASVDPK PAPAKRGRPA ASKPVKKDPV ISDDDESDVF
AAVAQEAAKE PSKSAAPSRA ARGATKQVAK YNLGSDSDDD EDLLGDVSSM VKTIGSATNG
VPMFKATTSA RPGSNGSARP GSSAVGKKSS TLEIDDNETN YEGLMPQPSP KRPAPRNVND
TIMSSDDDNS DLVIKKPAAS KLTAKPAAKS KTAAAKPVPK AKALAKKPAA QSPAAKAYAK
KHGKDAESAK PVPKAKKPIT IDSDDEDEEM EDADALANDI LSDEDEDEDE PTPKPAARKP
AAGAARPGRR AAAAKPAKYV VSDDDESDAV SEPSFDDDDD SE
//
