ID A0A0E0K969_ORYPU Unreviewed; 844 AA.
AC A0A0E0K969;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 22-FEB-2023, entry version 32.
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};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC03G04550.2};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC03G04550.2}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC03G04550.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0E0K969; -.
DR EnsemblPlants; OPUNC03G04550.2; OPUNC03G04550.2; OPUNC03G04550.
DR Gramene; OPUNC03G04550.2; OPUNC03G04550.2; OPUNC03G04550.
DR HOGENOM; CLU_002929_1_2_1; -.
DR Proteomes; UP000026962; Chromosome 3.
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:0008270; F:zinc ion binding; IEA:InterPro.
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; 2.
DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR023406; Topo_IA_AS.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
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 InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 2.
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.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
DR PROSITE; PS50158; ZF_CCHC; 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 Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 13..159
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 826..841
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 390..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 94646 MW; 3D3FD62DF51EC797 CRC64;
MHHGGDGGGG AIRVLNVAEK PSVAKSVAEI LSRPSGGMRS REGRSRYNRV FEFDYSIGGR
ACHMLVTSVT GHLMELEFDD RFRRWHSCDP ADLFHAPVRK SVPQDKQDIK RTLEEEARKC
QWLVLWLDCD REGENIAYEV IDICAGANSR LNIWRARFSA LIDREIHEAV QHLDRPNKLF
ADAVDARQEI DLRIGASFTR FQTMLLKDAF VLDDTGDDRN IVLSYGPCQF PTLGFIVERF
WEIQAHEPEE FWTINCSHTS DEGTATFGWM RGHLFDYSSA VVIYEMCVEE PMATVQNVRN
QEKLKYPPYP LSTIELQKRA SRYFRMSSEH TMKVAEELYQ AGFISYPRTE TDNFSQNTDL
HSIVHEQVAH PNWGTYAQRL LDPETRLWRN PSNGGHDDKA HPPIHPTKFS AGETNWTDNH
KKLYELVVRH FLACCSQPAV GAETTVEIDI AGEQFNASGR VKNYLDVYRF DSWGGTLLPT
YIIGQQAGIG TDATMHDHIK KLLDRCYATK DTNTRFSPTN LGEALVMGYD EMGYELWKPY
LRSMMEADMK SVSIGTKSKS EVLENCLQQM KACFLDARAN KVKLFDAMGT FFARSSRPVN
ETQNSIETVR PCAACNESEM VLKQRPCRNV VWLPRSLSEA AVTDQVCPTC APGPVYKIQF
KFRRRDIPPN FDVDHLGCIG GCDDVLKELM EISRFGSHSQ TATPARNQSQ TASAVRQGSS
RQDLHTSFRP AGQFINGQTP VVNPQGFRST HTQSSGNASD DVENSVPRGR GGRGRGGRSS
SRQSSASASA GRRGGTQGRG RRGRGRNNAD GMMFVAATGE PVHGSCFTCG DPTHFANVCP
NRGR
//
