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Database: UniProt
Entry: E3RFU2_PYRTT
LinkDB: E3RFU2_PYRTT
Original site: E3RFU2_PYRTT 
ID   E3RFU2_PYRTT            Unreviewed;       667 AA.
AC   E3RFU2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   22-FEB-2023, entry version 53.
DE   RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
DE            EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
GN   ORFNames=PTT_06616 {ECO:0000313|EMBL:EFQ95407.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ95407.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ95407.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
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|ARBA:ARBA00000213,
CC         ECO:0000256|RuleBase:RU362092};
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|RuleBase:RU362092}.
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DR   EMBL; GL532817; EFQ95407.1; -; Genomic_DNA.
DR   RefSeq; XP_003296497.1; XM_003296449.1.
DR   AlphaFoldDB; E3RFU2; -.
DR   STRING; 861557.E3RFU2; -.
DR   EnsemblFungi; EFQ95407; EFQ95407; PTT_06616.
DR   KEGG; pte:PTT_06616; -.
DR   eggNOG; KOG1956; Eukaryota.
DR   HOGENOM; CLU_002929_1_1_1; -.
DR   OrthoDB; 166270at2759; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
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:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR   Gene3D; 3.40.50.140; -; 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   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:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 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; 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, ECO:0000256|RuleBase:RU362092};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW   ECO:0000256|RuleBase:RU362092}.
FT   DOMAIN          3..148
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          540..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   667 AA;  74739 MW;  70D5094D8C0FB511 CRC64;
     MTRVLCVAEK PSIAKAVANH LGGQARAENV RGIQYVKNYK FDFRFNPWGD CSVTFTCVAG
     HIVHRDFNDQ FKKWHSCPPS ALFDAPIVSS IAQDKKIVAS NIEAQARYAS ILYIWTDCDR
     EGEHIGSQIR DIALKANPNM QVWRARFSNI ERAHVIQASQ NPIRLDEAQA EAVSARIELD
     LRLGAAFTRM QTFALQNMIP QQGEQRGKII SYGSCQFPTL GFVVDRYLRV RNFVPEPFWY
     IKVGHTKELE QTKDKVDVKF SWRRGHLFDR MAVTIIFEKC LLAKTAKVVK MAKKPTSKWK
     PLPLTTVELQ KMGSRFLRMT SQDVMKVAEE LYTKGWISYP RTETDQFDKA IDLRTLVGRQ
     TQDGRWGPFA QNLMNGGFHQ PRQGRNNDKA HPPIHPVNYV APTQLNDRER TVYEFVVRRF
     LACCSEDAVG EATDIEIDYG GEFFHAHGLT VMARNYLDVY PYDKWESSQV LPKYTVGETF
     EPTEASMQDG QTCAPNYLTE PELISLMDAN GIGTDATMAD HIDRIQMREY VIARAKGGGT
     AAAANGTGRG RGEGRGGRGG RGGRGGAAVG QDGGGGTSGV QEFIPTTLGV ALIEGYDNVG
     FETSLSKPFL RKEMEVQMKA ICEGRTTRND VVQQNLEKYR AVFNRTSQQI NVLKSAVTKY
     VVNANQG
//
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