ID A0A0G4IU69_PLABS Unreviewed; 736 AA.
AC A0A0G4IU69;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 03-MAY-2023, entry version 38.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
DE Flags: Fragment;
GN ORFNames=PBRA_006934 {ECO:0000313|EMBL:CEO98820.1};
OS Plasmodiophora brassicae (Clubroot disease agent).
OC Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC Plasmodiophoridae; Plasmodiophora.
OX NCBI_TaxID=37360 {ECO:0000313|EMBL:CEO98820.1, ECO:0000313|Proteomes:UP000039324};
RN [1] {ECO:0000313|EMBL:CEO98820.1, ECO:0000313|Proteomes:UP000039324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:CEO98820.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Introduces a single-strand break via transesterification at a
CC target site in duplex DNA. Releases the supercoiling and torsional
CC tension of DNA introduced during the DNA replication and transcription
CC by transiently cleaving and rejoining one strand of the DNA duplex. The
CC scissile phosphodiester is attacked by the catalytic tyrosine of the
CC enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme
CC intermediate and the expulsion of a 3'-OH DNA strand.
CC {ECO:0000256|RuleBase:RU362092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000213,
CC ECO:0000256|RuleBase:RU362092};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|RuleBase:RU362092}.
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DR EMBL; CDSF01000087; CEO98820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4IU69; -.
DR STRING; 37360.A0A0G4IU69; -.
DR EnsemblProtists; CEO98820; CEO98820; PBRA_006934.
DR OMA; MELAMGD; -.
DR OrthoDB; 166270at2759; -.
DR Proteomes; UP000039324; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013825; Topo_IA_cen_sub2.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362092};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW Reference proteome {ECO:0000313|Proteomes:UP000039324};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092}.
FT DOMAIN 3..161
FT /note="Toprim"
FT /evidence="ECO:0000259|SMART:SM00493"
FT DOMAIN 164..259
FT /note="DNA topoisomerase type IA"
FT /evidence="ECO:0000259|SMART:SM00436"
FT DOMAIN 307..573
FT /note="DNA topoisomerase type IA DNA-binding"
FT /evidence="ECO:0000259|SMART:SM00437"
FT NON_TER 736
FT /evidence="ECO:0000313|EMBL:CEO98820.1"
SQ SEQUENCE 736 AA; 82123 MW; B36A96234575A6DF CRC64;
MVVVLNVAEK PSVAKEVARV LSRGTAQQRT GPSPYNPVFE FQFDLQGQRV LMVFTSVLGH
VMRIDFVPPY DRGWSTCDPG DLFQAPIVKS LQPTMDKVNL NLEQQTRRAD KLVLWLDCDR
EGFARARLCV PPALRRPTLN VDRRRENISF EVVQICRSTR PHLPVLRARF SSLIPAELGR
ACQQLGPLNQ ALSQAVDVRT ELDLRIGAAF TRFQTLSFAH RFSGMPKVLS FGPCQFPTLG
FVVARHLQIE AFVPQDYWTI AMTWAEPGTR KTAQFRWVRG PLYDHAATLA FYQICVDAAV
ATVRHVRRFP TTRAKPLPLS TVPLQQNAAR RLRIGRAARA MAVCSNATMA AAEELYRRGL
ISYPRTETDS FLEGTDLMGM IRAQCASPVW GPFAQTLAGG RFAPPRQGGH NDMAHPPIHP
TQYVPLDSIG DVTERRIYEY VVRHFLACCS WDAQGDTTQV DVELGEEQFE CKGLQIRDLA
YMHVYTYETW TGNVIPTMAD GQRLVPTRLA INESRTAPPQ HLSEAELIGL MDRNGIGTDA
TIAQHIETIE KREYAVKRPD SRFAPTDLGL ALVTSYDSLG LHDLSTPRLR AMMEGDLTRI
AQGQAAPRDV LDRNLAEMKR VFAMVTSQKN RIASALSQRG TFPRYVACGA CNAAYRLPQY
GTCSAVDDHL CPLCAFQPIR IENVERGTTY TLCPFCSSES DIGSCLQCRE YRCRLAGGMS
PPVHRCPTCG TPSMGL
//
