(data stored in SCRATCH zone)

SWISSPROT: A8LF30_FRASN

ID   A8LF30_FRASN            Unreviewed;      1023 AA.
AC   A8LF30;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   RecName: Full=DNA topoisomerase 1 {ECO:0000256|HAMAP-Rule:MF_00952};
DE            EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00952};
DE   AltName: Full=DNA topoisomerase I {ECO:0000256|HAMAP-Rule:MF_00952};
GN   Name=topA {ECO:0000256|HAMAP-Rule:MF_00952};
GN   OrderedLocusNames=Franean1_0309 {ECO:0000313|EMBL:ABW09775.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09775.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- FUNCTION: Releases the supercoiling and torsional tension of DNA,
CC       which is introduced during the DNA replication and transcription,
CC       by transiently cleaving and rejoining one strand of the DNA
CC       duplex. Introduces a single-strand break via transesterification
CC       at a target site in duplex DNA. The scissile phosphodiester is
CC       attacked by the catalytic tyrosine of the enzyme, resulting in the
CC       formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the
CC       expulsion of a 3'-OH DNA strand. The free DNA strand then
CC       undergoes passage around the unbroken strand, thus removing DNA
CC       supercoils. Finally, in the religation step, the DNA 3'-OH attacks
CC       the covalent intermediate to expel the active-site tyrosine and
CC       restore the DNA phosphodiester backbone. {ECO:0000256|HAMAP-
CC       Rule:MF_00952}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-independent breakage of single-stranded DNA, followed
CC         by passage and rejoining.; EC=5.6.2.2;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00952,
CC         ECO:0000256|SAAS:SAAS01165083};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00721088};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952,
CC       ECO:0000256|SAAS:SAAS00709415}.
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00952, ECO:0000256|SAAS:SAAS00721110}.
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DR   EMBL; CP000820; ABW09775.1; -; Genomic_DNA.
DR   RefSeq; WP_012157752.1; NC_009921.1.
DR   STRING; 298653.Franean1_0309; -.
DR   EnsemblBacteria; ABW09775; ABW09775; Franean1_0309.
DR   KEGG; fre:Franean1_0309; -.
DR   eggNOG; ENOG4105C73; Bacteria.
DR   eggNOG; COG0550; LUCA.
DR   eggNOG; COG1754; LUCA.
DR   HOGENOM; HOG000004020; -.
DR   KO; K03168; -.
DR   OMA; IDFPGFF; -.
DR   OrthoDB; 223233at2; -.
DR   BioCyc; FSP298653:G1G9X-308-MONOMER; -.
DR   Proteomes; UP000001313; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003917; F:DNA topoisomerase type I 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   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03363; TOPRIM_TopoIA_TopoI; 1.
DR   Gene3D; 1.10.290.10; -; 1.
DR   Gene3D; 1.10.460.10; -; 1.
DR   Gene3D; 2.70.20.10; -; 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   PANTHER; PTHR42785; PTHR42785; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF13368; Toprim_C_rpt; 4.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF56712; SSF56712; 1.
DR   TIGRFAMs; TIGR01051; topA_bact; 1.
DR   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8LF30.
DR   SWISS-2DPAGE; A8LF30.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001313};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00952,
KW   ECO:0000256|SAAS:SAAS00721076};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00952,
KW   ECO:0000256|SAAS:SAAS00721131, ECO:0000313|EMBL:ABW09775.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00721141};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00721137};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001313};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00952,
KW   ECO:0000256|SAAS:SAAS00721067}.
FT   DOMAIN       76    200       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   REGION      249    254       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   ACT_SITE    401    401       O-(5'-phospho-DNA)-tyrosine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00952}.
FT   SITE        106    106       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        225    225       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        226    226       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        229    229       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        234    234       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        241    241       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        403    403       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        603    603       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
SQ   SEQUENCE   1023 AA;  109236 MW;  FC9CF8DEAC4D2977 CRC64;
     MPPRTNSTSR TTAGSPTPVA EPTKPAAASA TAASATAAKA EAAETAEAGA TAGRASGARA
     TGGRRPARAT TNGNGTRLVI VESPAKAKTI AGYLGPGWQV ESSIGHIRDL PRSAADVPTA
     HKGKPWARLG VDVDNGFEPL YVVSPDKKVQ VSKLKSLVKD ASELYLATDE DREGEAIAWH
     LLQTLKPTVP VKRMVFHEIT PQAIQRAVDS PREINENLVN AQETRRILDR LYGYEVSPVL
     WKKVMPKLSA GRVQSVATRI LVERERARMR FRTAEYWNIE GVFQQNVAHD GAALDTTPLP
     ATLVALDGRR LASGRDFAPT GELTSDGVAL LDEAGARALA GRLTGAAFAV RSVETKPYRR
     SPYPPFMTST LQQEAGRKLR FSSQRTMQVA QRLYENGYIT YMRTDSTNLS ETALVAARDQ
     ARTLYGAEYV PDRPRVYAKK VKNAQEAHEA IRPAGDHFRT PGEVRSELDG DSFRLYELIW
     QRTVASQMAD ARGTSATIRL GATSSSGEDA EFSASGKVIT FPGFLRAYVE GADDPDAELE
     DRERRLPDVR RGDPLATRTL TPRGHTTSPP PRFTEASLVK TLEELGIGRP STYASIIGTI
     QDRGYVWKKG SALVPSFVAF AVVGLLEDHF TRLVDYQFTA SMEDDLDAIA AGTAASTDWL
     TGFYFGLPDT TDTGGSGAVE GLKHLVGERL GEIDAREVNS IPLGKADDGE PVVVRVGRYG
     PYVQHADGRA SVPDEVAPDE LTVERALELL AAPSGDRLLG TDPKTGASIT AKAGRYGPYV
     TTDSEPPQTA SLLRTMSLET VTLEDALRLL TLPRVLGTDA EGAEVTAQNG RYGPYVKRGA
     DSRSLESEDQ LFTVTLDEAL ALLAQPKARG RRQAAQTPPL RELGPDPATE RPMVLREGRF
     GPYVTDGETN ASLRKGDAVE TITVERAAEL LADRRARGTT TPRRTTKTTA KAPAKATAKP
     RTAAKTTTKA KTAGKTSGGT AKSGSRASKS AASDAGATGT AAGDASGTDS ATGATSGGSQ
     RSS
//

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