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Database: UniProt
Entry: A0A1D6LWZ0_MAIZE
LinkDB: A0A1D6LWZ0_MAIZE
Original site: A0A1D6LWZ0_MAIZE 
ID   A0A1D6LWZ0_MAIZE        Unreviewed;      1200 AA.
AC   A0A1D6LWZ0;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE            EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
GN   ORFNames=ZEAMMB73_Zm00001d037362 {ECO:0000313|EMBL:AQK83746.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK83746.1};
RN   [1] {ECO:0000313|EMBL:AQK83746.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK83746.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00009446}.
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DR   EMBL; CM000782; AQK83746.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6LWZ0; -.
DR   SMR; A0A1D6LWZ0; -.
DR   IntAct; A0A1D6LWZ0; 1.
DR   STRING; 4577.A0A1D6LWZ0; -.
DR   InParanoid; A0A1D6LWZ0; -.
DR   ExpressionAtlas; A0A1D6LWZ0; baseline and differential.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03363; TOPRIM_TopoIA_TopoI; 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   HAMAP; MF_00952; Topoisom_1_prok; 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; IPR005733; TopoI_bac-type.
DR   InterPro; IPR028612; Topoisom_1_IA.
DR   InterPro; IPR025589; Toprim_C_rpt.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034149; TOPRIM_TopoI.
DR   NCBIfam; TIGR01051; topA_bact; 1.
DR   PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR   PANTHER; PTHR42785:SF1; OMEGA-PROTEIN; 1.
DR   Pfam; PF01131; Topoisom_bac; 2.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF13368; Toprim_C_rpt; 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.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AQK83746.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
SQ   SEQUENCE   1200 AA;  135694 MW;  63EBBA45D14974F8 CRC64;
     MALQLRRLLP HGYAQRHRAV IHALSLLPPP PAMLQFEVFQ RYSSSPWPFS PFRPCKMCGV
     AFRSNSTRKI SSRNNFGVAL QPKSSAFITP RLFGSYSSVC FRATASCGIA LKANNIGNSR
     PFSTTYSKKI RFLVKNKISF SNLNMRRKDG SVAHSLLHRS EKCQSTLATC STIVDEASTS
     TSNNSKSVTD AKTDTAKRKS SRGSKKEVDG DMKEKEVHTN KKRIFARTRK AATKTSDNIS
     TNQENKKTDN CKLKRGADSF KEKKVNNRAK SKAEVSAASS VPEICMQSSI DGSVIEKKPL
     VPLYPPRAKS VVVVESATKA KVIQKYLGDM YEVLPSYGHV RDLAGRSKSV RPDDDFSMVW
     EVPAAAWTHL KSIKVALQRA ENLILASDPD REGEAIAWHI KEMLEQQGVL GFDVTVARVV
     FHEISEDAIK KALMSPRYID MDLVNAYLAR RSLDYLIGFG ISPLLWRKLP GCQSAGRVQS
     AALALVCDRE AEIEQFKAHE YWTVQTDFKI QSADPSNATC IPFCIKHLNS KKLDQLSIPS
     QEEAQAIEKM IHSSTFEVLG VKRSKIHKNP PLPYITSSLQ QDAANKLHFT AGYTMKIAQN
     LYEGINLSSE ETTGLITYIR TDGFHISDGA VEDIRSLVKE RYGQKYVSED IRKYLKKVKN
     AQEAHEAIRP TSIRRPPSSL VGILDDDSLK LYTLIWKRTM ACQMEASRTE MVGYSRASFF
     YVVDFILHDD NGYELWVYKV TLVKETLISL TWHIQVDVGI PEGEMNFHST ASKLDFKGYR
     AVYEGPIVSA IAFSHLHDLL LVIRDDQASP CIDSSEGDCV HECNFEALSK LMVAVKDLVF
     PVNVHLGQHF TKPPPRYSEG ALIKKLEELG IGRPSTYASI MKVLLDRKYV TAKSRVLHPE
     FRGRMVCSYI PDCMFPVSAF LLHHFSEVSD YNFTANMETE VFKYFSAYVF YNVSAGSTEW
     KGLLKDYWER FSKYCADVSK LDGRKVERML EEKFGPILFS DVYKDCRICP SCSEGTLRFK
     VSRYGEGYFV GCDRHPKCKY IARSLSQQED ETEPIEENAK SFEPRLLGVM PDSDQKVFLK
     QGPYGYYVQV GEDKKGLFPK RVSLSKVKDI DSVTLEDAIE LLQYPKILGK HPEDDNLVLI
     THSKVGYNIK HRRFIAQVPK NMDPKKMTLE RALKLLSSKS VRRIGRLKGK VEKKEPIEWH
//
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