ID R4X883_TAPDE Unreviewed; 1525 AA.
AC R4X883;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=TAPDE_001558 {ECO:0000313|EMBL:CCG81723.1};
OS Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC Taphrinales; Taphrinaceae; Taphrina.
OX NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG81723.1, ECO:0000313|Proteomes:UP000013776};
RN [1] {ECO:0000313|EMBL:CCG81723.1, ECO:0000313|Proteomes:UP000013776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA Overmyer K., Hauser P.M., Pagni M.;
RT "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT agent of peach leaf curl.";
RL MBio 4:e00055-e00013(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}.
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:CCG81723.1}.
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DR EMBL; CAHR02000056; CCG81723.1; -; Genomic_DNA.
DR STRING; 1097556.R4X883; -.
DR VEuPathDB; FungiDB:TAPDE_001558; -.
DR eggNOG; KOG0355; Eukaryota.
DR Proteomes; UP000013776; 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; 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:UP000013776};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 519..633
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1368..1525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1525
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1525 AA; 171798 MW; 94FDAAF4A25B8926 CRC64;
MSSAGSDYEN YEPSPAVKKK VANLKRAKKV MDSDEESFQS PRPVAKKARI ATTAKTTRAI
STPLADVDPN HMMSDDSDAE QGVSSKTSAK KATKASDNYQ KLTQLEHVIK RPDTYIGSIE
SQQNEMWSYV PEKSAMEFKK ISLVPGLFKI YDEILVNAAD NKERDQNMDT LKVDFDRATN
TITVMNNGHG IPVEMHEKEG VYIPELIFGH LLTSSNYDDD KKKTTGGRNG YGAKLANIFS
TEFTLETTDQ KNGKKYVQTW TQNMSKMSKP KITSWKSAEY TKITFKPDLQ KFGMLEMDDD
LEGIFQRRVY DLAGCVPGIK VFLNGERIKI KTFKEYANMY IASLPPAEKP PPLIYERVND
RWEVAFTISE GQFNQVSFVN SIATTKGGTH VNYIADQIVK RIIEEYAKKN KKASALKAFQ
VKQHIWLFVN CKIENPAFDS QTKETLTLKA SQFGSKCNLG DDFMKKVLKS GVLDDITRQS
EMRADKAMKK TDGAKRTRIT GMAKLEDANK AGTREAERCT LILTEGDSAK TLAISGMSVV
GRDHFGVFPL RGKLLNVRDA AANQVSANTE IQNIKQILGL KHGVKYKDAK ELRYGHLMIM
TDQDHDGSHI KGLIINYLEC FYPSLLSIPG FLIEFITPIV RCTKGKEVVS FFTIPEYEAW
KEDVQPGKEW KIKYFKGLGT SDTADAKKYF SDLDKHLKEF HTLQDGDQDL ISLAFSKHRA
DDRKEWLRKF VPGTYMDHSM TKIPFKNFIN DELILFSMAD NIRSIPNVMD GFKPGQRKIL
FACFKRKLKA EIKVAQLVGY VGEHTAYHHG EQSLSQTIVG LAQSFVGSNN INILMPNGQF
GTRHSGGKDA ASARYIFTDI AKIARKIFVE PDSPLLNYLN DDGLMVEPQW FAPILPMILV
NGAQGIGTGW STSIPNFNPA DLVRNIRKLM DGEEIKPMEP WYRGFQGLIE EDPKQKGYRA
QGIVHEIDDT TVEITELPLG FWTLDMKEFL EQAIAGTDKS PPWVKDYADN STESRIHFTI
TLTDKSMKDA LHTGLLEKFK LTKNISMQNL VAFDPDGRIR KYNSAEEILK EFYHIRLQFY
QRRKDWMAAD LEKQYDRLSN QARFVQMIIN KELSVSNKKR AALVDELKAL KFTPFPTKKT
AQVAGETEES LEDDAEENAE KHSDHGYDYL LGMAIWSLTR ERVEKLLKDR AHKEEELNSL
LKRSAKDLWK SDLDDFELEW QKLLENDEAL ASKTDTIRKK AKGTKLAGKS KAPAKRKKAG
SDDDASDDDF TPVKKRLPEV KKEKPRATKL HDDKIEVKDE PSPEILPPKK VTALKQAKLK
LESQTKKILQ TDDSPVALLS DKSDKSHTLS ADSDEDDVYN FVAKTAATKK TAGQEKKNLP
KTVPIRRDDS DSDDWMAKFT EPKPKSTITR VPQIQTSTLE SEDEAPAASV SKEVAAPEAD
HGAKRTMATK KTSRPPASSK SQVTEKSKND HAKPVPAVVK RPGRAAANAR KVVVESDDDV
EADQDSDVSI DAGDVSEDFF DDDED
//
