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Database: UniProt
Entry: A0A251RD54_PRUPE
LinkDB: A0A251RD54_PRUPE
Original site: A0A251RD54_PRUPE 
ID   A0A251RD54_PRUPE        Unreviewed;      1176 AA.
AC   A0A251RD54;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE            EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
GN   ORFNames=PRUPE_1G457500 {ECO:0000313|EMBL:ONI33989.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI33989.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI33989.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(2013).
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; CM007651; ONI33989.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251RD54; -.
DR   STRING; 3760.A0A251RD54; -.
DR   EnsemblPlants; ONI33989; ONI33989; PRUPE_1G457500.
DR   Gramene; ONI33989; ONI33989; PRUPE_1G457500.
DR   eggNOG; KOG1956; Eukaryota.
DR   OrthoDB; 167550at2759; -.
DR   Proteomes; UP000006882; Chromosome g1.
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; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 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   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; 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; 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:SF1; DNA TOPOISOMERASE; 1.
DR   PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF13368; Toprim_C_rpt; 2.
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};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          363..478
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          236..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1021..1043
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1153..1176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..337
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1161..1176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1176 AA;  130281 MW;  C835453177C98D38 CRC64;
     MAMIHFQRTL SLTAPTSSAS SFVCSNTLAS SALRLRRSMA KLQYRAFETY PCVCLPSSPI
     LTASKYRNYS QLKLKKSGGS CMIMINPAKV GPSFHSFRRS GDGSERAFSN LKPGSLNSLG
     PGNVISPGSF GSVANYSIGG FAKRFFSQVP HVTSKLESVG AQNGKYSVST SFFKQLSKRR
     KREKALAAQS KNEATISSIS KDVDVEASTE RQIGSEKGDG KLGSFLSNSL IINDNHVPKV
     KGKKRSKSKK TKEQISAANA PAEAAATQSS KGTSQTKKSG STKSGKKSAQ DSELNFTGKV
     PVEISDGSSI KPQPKKKSGN SSRKGKSITS DSKSPQKHIP QKMGKVKPQG KMTLKQLYPA
     TGRTVVVVES ATKAKVIQGY LGDMFEVLPS YGHVRDLAAR SGSVRPDDDF SMVWEVPSAA
     WTHLKSIKVA LTGAENLILA SDPDREGEAI AWHIIEMLQQ QDALREDINV ARVVFHEITE
     TSIKSALQAP REIDENLVHA YLARRALDYL IGFNISPLLW RKLPGCQSAG RVQSAALALL
     CDREMEIDEF KQQEYWTAEI ELNQKEPGSS VNAPDFSAHL THFDSKKLNQ FSIDSHTKAK
     EIEQQINSQN FQVVSSKKNK MRKNPPTPYI TSTLQQDAAN KLHFSAAYTM KLAQKLYEGV
     QLSDGKAAGL ITYMRTDGLH ISDEACKDVR SLVIQRYGQN FASESPRKFF KKVKNAQEAH
     EAIRPTDVRR LPSLFRGMLD EDSLKLYTLI WCRTVACQME PATIEQIQLD IGNAGESIVF
     RSSCSRVEFL GYQAVFEDVE AQAVKYKENE GNSRNEGFGL LNSLKRGDPL YVGKVELKEH
     HTQPPARYSE ASLVKKLEEL GIGRPSTYAS TLKVLQDRNY VTVKSRVLHP EFRGRMVSAF
     LGHHFSEVTD YSFTADMETE LDNVSAGLTE WKGLLRDYWT RFSAYCDRTS TVHIHQVEKM
     MEKKFGDFLF ASLPDQSRTC PCCMEGNLIF KVSRFGAGYF IGCDQHPKCK YIAKTLYGDD
     EEEESTPKNS SMEEPKVLGL SPGSNEKVLL KNGPYGSYVQ LGEDRKGNSP KRASVSHIKD
     VGSITLEDAL ELMRYPVTLG NHPEDGQPVI IKVARVGFAV RHRRTIASVP KVYKNKKPSE
     ITLEDALELL SSSNVRRSGR PKSKPKVEEE VMLEAV
//
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