(data stored in ACNUC6288 zone)

SWISSPROT: Q6BLX2_DEBHA

ID   Q6BLX2_DEBHA            Unreviewed;       789 AA.
AC   Q6BLX2;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   08-MAY-2019, entry version 99.
DE   RecName: Full=DNA topoisomerase I {ECO:0000256|RuleBase:RU365101};
DE            EC=5.6.2.2 {ECO:0000256|RuleBase:RU365101};
DE   AltName: Full=DNA topoisomerase 1 {ECO:0000256|RuleBase:RU365101};
GN   OrderedLocusNames=DEHA2F09988g {ECO:0000313|EMBL:CAG89140.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89140.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89140.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Releases the supercoiling and torsional tension of DNA
CC       introduced during the DNA replication and transcription by
CC       transiently cleaving and rejoining one strand of the DNA duplex.
CC       Introduces a single-strand break via transesterification at the
CC       specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile
CC       phosphodiester is attacked by the catalytic tyrosine of the
CC       enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-
CC       enzyme intermediate and the expulsion of a 5'-OH DNA strand. The
CC       free DNA strand then undergoes passage around the unbroken strand
CC       thus removing DNA supercoils. Finally, in the religation step, the
CC       DNA 5'-OH attacks the covalent intermediate to expel the active-
CC       site tyrosine and restore the DNA phosphodiester backbone.
CC       {ECO:0000256|RuleBase:RU365101}.
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|RuleBase:RU365101};
CC   -!- SIMILARITY: Belongs to the type IB topoisomerase family.
CC       {ECO:0000256|RuleBase:RU365101}.
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; CR382138; CAG89140.2; -; Genomic_DNA.
DR   RefSeq; XP_460799.2; XM_460799.1.
DR   STRING; 4959.XP_460799.2; -.
DR   EnsemblFungi; CAG89140; CAG89140; DEHA2F09988g.
DR   GeneID; 2904211; -.
DR   KEGG; dha:DEHA2F09988g; -.
DR   HOGENOM; HOG000105469; -.
DR   InParanoid; Q6BLX2; -.
DR   KO; K03163; -.
DR   OMA; CSLKYEH; -.
DR   OrthoDB; 303947at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:EnsemblFungi.
DR   GO; GO:0000183; P:chromatin silencing at rDNA; IEA:EnsemblFungi.
DR   GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IEA:EnsemblFungi.
DR   GO; GO:0007097; P:nuclear migration; IEA:EnsemblFungi.
DR   GO; GO:0000019; P:regulation of mitotic recombination; IEA:EnsemblFungi.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   CDD; cd00659; Topo_IB_C; 1.
DR   Gene3D; 1.10.10.41; -; 1.
DR   Gene3D; 1.10.132.10; -; 1.
DR   Gene3D; 2.170.11.10; -; 1.
DR   Gene3D; 3.90.15.10; -; 1.
DR   InterPro; IPR011010; DNA_brk_join_enz.
DR   InterPro; IPR013034; DNA_topo_DNA_db_N_dom1.
DR   InterPro; IPR013030; DNA_topo_DNA_db_N_dom2.
DR   InterPro; IPR001631; TopoI.
DR   InterPro; IPR018521; TopoI_AS.
DR   InterPro; IPR025834; TopoI_C_dom.
DR   InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR   InterPro; IPR014727; TopoI_cat_a/b-sub_euk.
DR   InterPro; IPR013500; TopoI_cat_euk.
DR   InterPro; IPR008336; TopoI_DNA-bd_euk.
DR   InterPro; IPR036202; TopoI_DNA-bd_euk_N_sf.
DR   InterPro; IPR013499; TopoI_euk.
DR   Pfam; PF14370; Topo_C_assoc; 1.
DR   Pfam; PF01028; Topoisom_I; 1.
DR   Pfam; PF02919; Topoisom_I_N; 1.
DR   PRINTS; PR00416; EUTPISMRASEI.
DR   SMART; SM00435; TOPEUc; 1.
DR   SUPFAM; SSF56349; SSF56349; 1.
DR   SUPFAM; SSF56741; SSF56741; 1.
DR   PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BLX2.
DR   SWISS-2DPAGE; Q6BLX2.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   DNA-binding {ECO:0000256|RuleBase:RU365101};
KW   Isomerase {ECO:0000256|RuleBase:RU365101};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Topoisomerase {ECO:0000256|RuleBase:RU365101}.
FT   DOMAIN      313    761       TOPEUc. {ECO:0000259|SMART:SM00435}.
FT   COILED      674    697       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   789 AA;  90565 MW;  A48321228E216245 CRC64;
     MMSSSDDNVA LSMIDGNIDQ DDDMPLSQIS SKSTDTTSVD SNSTEGQKSG SKRKASSPTG
     HKAKKVKRSK NTVKSESDEE NTPLASTTAP PPKKTSKKKS ESGTAKPRNG TKKSKGAKST
     GSNKTDAVKK EDEVAKTEKD PSSTREDEED EEKYKWWEAE DVDGEQKWES LEHNGVIFPP
     DYEPLPSHVK LYYDGKPVDL PLEAEEVAGF FGAMAETDHA KNPTFQKNFF EDFCKVLKDA
     GGCNVNIIDF HRMDFSKMHA HFEMLRDQKK LLSKDEKKAI KAEKDKFEEP YKTCLLNGHK
     EQVGNFRIEP PGLFRGRGAH PKTGKLKRRV MPEDVTLNLS EGCKIPEPPQ GHKWAEVRHD
     NTVSWLAMWK ENIADSFKYV RFAANSSIKG LSDFKKFETS RKLRYHIDEI RKDYTKMLKD
     PLMQNRQMAT ACYLIDIFAL RAGGEKGDDE ADTVGCCSLR YEHITLKPPN KVIFDFLGKD
     SIRFYQEVEV EKQVFKNLRI FKKPPKQPGD DLFDRISPPL LNKQFQNYMK GLTAKVFRTY
     NASKTMQDQL DLIPNEGTVA EKVVKFNAAN RTVAILCNHQ RTVSKTHGSS VQKIHDKLKE
     LEWHKIRTKK MILQLEPNLK TKDPDYFEEL DDLSKEDTEH IHRALIERAR EAARKRFQRE
     NDKLKIEDKP LLTEKDLEEK MEKVNELEKE YAEELKTGKP QIKKSVTVEK LKSQVDTLTN
     RILNTTFQLK DKEDNSEVSL GTSKMNYIDP RLTVMFSKKF NVPIEKLFTK TLRDKFNWAI
     ESADENWKF
//

If you have problems or comments...

PBIL Back to PBIL home page