(data stored in ACNUC1104 zone)

SWISSPROT: A4F6Q1_SACEN

ID   A4F6Q1_SACEN            Unreviewed;       922 AA.
AC   A4F6Q1;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 96.
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   ECO:0000313|EMBL:CAL99725.1};
GN   OrderedLocusNames=SACE_0377 {ECO:0000313|EMBL:CAL99725.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99725.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99725.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AM420293; CAL99725.1; -; Genomic_DNA.
DR   RefSeq; WP_009946467.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0377; -.
DR   EnsemblBacteria; CAL99725; CAL99725; SACE_0377.
DR   KEGG; sen:SACE_0377; -.
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; SERY405948:SACE_RS01845-MONOMER; -.
DR   Proteomes; UP000006728; 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; A4F6Q1.
DR   SWISS-2DPAGE; A4F6Q1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728};
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:CAL99725.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00721141};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00721137};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00952,
KW   ECO:0000256|SAAS:SAAS00721067}.
FT   DOMAIN        1    123       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   REGION      172    177       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   ACT_SITE    319    319       O-(5'-phospho-DNA)-tyrosine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00952}.
FT   SITE         29     29       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        149    149       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        152    152       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        157    157       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        164    164       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        321    321       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
FT   SITE        522    522       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_00952}.
SQ   SEQUENCE   922 AA;  101154 MW;  8D72B8139DA7A90E CRC64;
     MVIVESPAKA RKIASYLGSN FVVESSRGHI RDLPSGAADV PAKYKGQPWA RLGVDVDNDF
     EPLYLVTPDK KATVTELKDA LKEVDELYLA TDGDREGEAI AWHLMETLKP KVPVRRMVFH
     EITESAIQSA AANPRELDRD LVDAQETRRI LDRLYGYEVS PVLWKKVMPK LSAGRVQSVA
     TRIVVERERE RIKFVPAEYW DISATMDAGP DAEPRRFGAR LVSVDGAKLA TGRDFGPDGR
     LKNDDVRLLN EAEARRLATG LTDARLSVSS VEEKPYTRKP YAPFMTSTLQ QEASRKLRFS
     ADRTMRTAQR LYENGYITYM RTDSTTLSET AITAARNQAR DLYGDEYLSP QPRQYNRKVK
     NAQEAHEAIR PAGESFRTPG QVAAELDTDG YKLYELIWQR TIASQMADAK GTTLSVRITG
     TSADGEECTF AASGRTITFA GFLKAYVEAV DSEAGGVADD AESRLPRLAQ YQAVTAPELS
     PDGHSTNPPP RYTEASLVKA LEELGIGRPS TYASIISTVQ DRGYVWKKGS ALVPSWVAFA
     VVGLMEKHFG RLVDYDFTAA LEDELDRIAE GRQQRTKWLS GFYFGGEVGP DDSIGRAGGL
     KKLVGSSVEE IDAREVNSIP MFTDDDGRTV YVRVGRYGPY LERPLSDSES QRANLPDDLP
     PDELDIQIAE KLFATPMEGR SLGTDPETGH EVLAKEGRFG PYVTEVLPEG SKGKPRTGSL
     LKSMSLDTVT IDDALKLLAL PRVVGTDPES GTEITAQNGR FGPYLKRGSD SRSLDTEEQI
     FTVTLEEALK LYAQPKQRGR RAAAAPLREL GDDPDSGKPL VIKDGRFGPY VTDGETNASL
     RKGDSVEELT IDRAVELIAE RRAKAPAKKK TASKSKSTAS KSTSSKTTAS KSSSSKSSSS
     NGSKTTKSGT TRKRTTSSSK QS
//

If you have problems or comments...

PBIL Back to PBIL home page