(data stored in ACNUC7421 zone)

SWISSPROT: Q751B3_ASHGO

ID   Q751B3_ASHGO            Unreviewed;       631 AA.
AC   Q751B3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 115.
DE   RecName: Full=DNA topoisomerase {ECO:0000256|RuleBase:RU362092};
DE            EC=5.6.2.1 {ECO:0000256|RuleBase:RU362092};
GN   ORFNames=AGOS_AGL101C {ECO:0000313|EMBL:AAS54390.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54390.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54390.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Introduces a single-strand break via transesterification at a
CC       target site in duplex DNA. Releases the supercoiling and torsional
CC       tension of DNA introduced during the DNA replication and transcription
CC       by transiently cleaving and rejoining one strand of the DNA duplex. The
CC       scissile phosphodiester is attacked by the catalytic tyrosine of the
CC       enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme
CC       intermediate and the expulsion of a 3'-OH DNA strand.
CC       {ECO:0000256|RuleBase:RU362092}.
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|RuleBase:RU362092};
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|RuleBase:RU362092}.
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DR   EMBL; AE016820; AAS54390.1; -; Genomic_DNA.
DR   RefSeq; NP_986566.1; NM_211628.1.
DR   STRING; 33169.AAS54390; -.
DR   EnsemblFungi; AAS54390; AAS54390; AGOS_AGL101C.
DR   GeneID; 4622865; -.
DR   KEGG; ago:AGOS_AGL101C; -.
DR   HOGENOM; HOG000184377; -.
DR   InParanoid; Q751B3; -.
DR   KO; K03165; -.
DR   OMA; TYPRVDT; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031422; C:RecQ family helicase-topoisomerase III complex; IEA:EnsemblFungi.
DR   GO; GO:0035861; C:site of double-strand break; IEA:EnsemblFungi.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003916; F:DNA topoisomerase activity; IBA:GO_Central.
DR   GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
DR   GO; GO:0043007; P:maintenance of rDNA; IEA:EnsemblFungi.
DR   GO; GO:1902969; P:mitotic DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:EnsemblFungi.
DR   GO; GO:0006301; P:postreplication repair; IEA:EnsemblFungi.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IEA:EnsemblFungi.
DR   GO; GO:0000018; P:regulation of DNA recombination; IEA:EnsemblFungi.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; IEA:EnsemblFungi.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR   Gene3D; 1.10.290.10; -; 1.
DR   Gene3D; 1.10.460.10; -; 1.
DR   Gene3D; 2.70.20.10; -; 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; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034144; TOPRIM_TopoIII.
DR   PANTHER; PTHR11390; PTHR11390; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
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   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q751B3.
DR   SWISS-2DPAGE; Q751B3.
KW   DNA-binding {ECO:0000256|RuleBase:RU362092};
KW   Isomerase {ECO:0000256|RuleBase:RU362092};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Topoisomerase {ECO:0000256|RuleBase:RU362092}.
FT   DOMAIN          2..148
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   631 AA;  71859 MW;  EFAC302162A68914 CRC64;
     MRVVCVAEKN SIAKAVAGIL GGGNTRTRSS PSKYIKNYDF TYNFAWAQGG ERCEVTMTAV
     AGHLMSQDFG PQYGWNKCDP RELFGAEILE TPTREIAENI TRECRGAEYL MIWTDCDREG
     EAIGWEIARV AMQANTRLVR SRIHRAVFSH LGREHIMRAA NSPSQIDMNA VDAVKARSEI
     DLRAGYAFTR LLTATLRAKV EQDMPAANEK KRALISYGTC QFPTLGFVVD RYERIQNFVS
     EGFWYLQLLI EDPQCARKVT FSWDRGHLFD RLCVLCLYET CIEATGNKAL VSSVTAKDTS
     KYRPLPLTTV ELQKNCSKFL RMSAKQSLDA AEKLYQKGFI SYPRTETDVF SKQANLQGLV
     QQQTEHSQWG AYASKLLSGE GSNRFQWPRE GKHDDQAHPP IHPVLCAQPD ANLSVDEKRV
     YEYVVRHFLA CCSQDAKGRS SKIKLKWHTE EFSATGLQVH EENFLEIYTY QKWTSSEQLP
     TLPLNSQVEF AKAEMKSGKT SPPKYITESE LIMLMDANGI GTDATIAEHI EKIQERQYIK
     AEGTAKNKVF KPTMLGRSLV HGFEDIGLEE SFAKPFLRRD MELDLKRICE GTKDRNSVLA
     NLIGMYMDYY DQTDRQRSKL IHCYERIKQE S
//

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