(data stored in ACNUC7421 zone)

SWISSPROT: A0LER2_SYNFM

ID   A0LER2_SYNFM            Unreviewed;       767 AA.
AC   A0LER2;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 97.
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=Sfum_0213 {ECO:0000313|EMBL:ABK15914.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15914.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15914.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000478; ABK15914.1; -; Genomic_DNA.
DR   RefSeq; WP_011697087.1; NC_008554.1.
DR   STRING; 335543.Sfum_0213; -.
DR   EnsemblBacteria; ABK15914; ABK15914; Sfum_0213.
DR   KEGG; sfu:Sfum_0213; -.
DR   eggNOG; ENOG4105C73; Bacteria.
DR   eggNOG; COG0550; LUCA.
DR   eggNOG; COG0551; LUCA.
DR   HOGENOM; HOG000004018; -.
DR   KO; K03168; -.
DR   OMA; PECKYTR; -.
DR   OrthoDB; 223233at2; -.
DR   BioCyc; SFUM335543:G1G7I-216-MONOMER; -.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
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; IPR013498; Topo_IA_Znf.
DR   InterPro; IPR005733; TopoI_bac-type.
DR   InterPro; IPR028612; Topoisom_1_IA.
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; PF01396; zf-C4_Topoisom; 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; A0LER2.
DR   SWISS-2DPAGE; A0LER2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
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:ABK15914.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00721141};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00721137};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00952,
KW   ECO:0000256|SAAS:SAAS00721067}.
FT   DOMAIN        3    114       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   REGION      163    168       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   ACT_SITE    308    308       O-(5'-phospho-DNA)-tyrosine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00952}.
FT   SITE         33     33       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        139    139       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        140    140       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        143    143       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        148    148       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        155    155       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        310    310       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        502    502       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
SQ   SEQUENCE   767 AA;  85422 MW;  5E0D77E8AC17197F CRC64;
     MSKSLLIVES PTKAKTLGRY LGKDFIVKAS VGHVKDLPKN RLGINLEKDF QPEYQVIRGK
     KKVISELHEA AAKSGAIFLG PDPDREGEAI AWHIAEEIGA TDKPVYRVLF YELTRKAIQE
     ALAKPDRLNR ELYEAQQARR ILDRLVGYMI SPILWQKVKR GLSAGRVQSV ALRLICAREK
     EIRDFDSREY WTITALLGTQ ASADAPAKSA SRRFKAELFR CGKKKCTIST GEEARELVDR
     LRPLDYRVSK VERRKKKRHP APPFITSTLQ QEAARKLHFS ARQTMNVAQR LYEGLELGKE
     GAVGLITYMR TDSTRLSADA VQAVRDYIAG HWDKAYLPAK PAAYKSKAGA QGAHEAIRPT
     DVNRTPETVA GFLTKEQLKL YTLIWKRFTA CQMAPAVLDQ TSVDIAAGDY VLRASGSIVE
     FPGFMTLYVE GRENGDEDSE TEGLLPELKE GEVLRLEDLK ADQHFTQPPP RYTEASLIKE
     LEDLGIGRPS TYATILSTIL DREYAVVRKK SLFPSELGWL IDGLMVENFP SVVDVDFTAK
     MEKSLDEIEQ GQHPYRNLLA EFYEQFSKTL ESARTNMVNL KAVGRRTDLQ CPQCGLPLHI
     RWSRNGPFLA CSGYPDCRFS SDYRRDEKGN IEPVAEESTG ETCEKCGRPM ILKKGRFGNF
     LACSGYPACK NTKAPGTGIP CPREGCSGEL VERVSRGGRH FFGCSRYPEC KTAFSGRPVP
     GKCPSCGTGP LIEKGGKGGS VKRVCVNPSC KYVETVPAAA DRKAAKD
//

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