ID B5RU11_DEBHA Unreviewed; 732 AA.
AC B5RU11;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=DEHA2E13706p {ECO:0000313|EMBL:CAR65823.1};
GN OrderedLocusNames=DEHA2E13706g {ECO:0000313|EMBL:CAR65823.1};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAR65823.1, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAR65823.1, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., 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 ---------------------------------------------------------------------------
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; CR382137; CAR65823.1; -; Genomic_DNA.
DR RefSeq; XP_002770480.1; XM_002770434.1.
DR AlphaFoldDB; B5RU11; -.
DR STRING; 284592.B5RU11; -.
DR GeneID; 8998748; -.
DR KEGG; dha:DEHA2E13706g; -.
DR VEuPathDB; FungiDB:DEHA2E13706g; -.
DR eggNOG; ENOG502QPWC; Eukaryota.
DR HOGENOM; CLU_390837_0_0_1; -.
DR InParanoid; B5RU11; -.
DR OMA; WIPYDKA; -.
DR OrthoDB; 3019647at2759; -.
DR Proteomes; UP000000599; Chromosome E.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:UniProt.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.10.260.10; Transcription regulator HTH, APSES-type DNA-binding domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA/APSES_HTH.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR PANTHER; PTHR43828; ASPARAGINASE; 1.
DR PANTHER; PTHR43828:SF3; REGULATORY PROTEIN SWI6; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF04383; KilA-N; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF54616; DNA-binding domain of Mlu1-box binding protein MBP1; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 44..169
FT /note="HTH APSES-type"
FT /evidence="ECO:0000259|PROSITE:PS51299"
FT REPEAT 422..454
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 182..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 82261 MW; 2EF3C91E2FEE859F CRC64;
MDSPLNVGDT TTNSIQHLLS DTHLNTSCST TVNSAVYSDE KVIQLNLVIQ TNEKEDGRKK
EDDPIVILRR VQDSYINISQ LFSILLKIGH LSEAQLTNFL NNEILTNTQY LSSGGSNPQF
NDLRNHEVRD LRGLWIPYDR AVSLALKFDI YELAKSLFLI DVHDYDDLPK VVTANKRSLY
EGSADGEKDA GLTGSPSKKQ KIQADKMNGD QADIQSILKK TIQENKSFPR TLPPLASDEE
NSELESDIKS KFSEIFKKDN TSELSYTDIK STFQNILQNK QENLRLLTDI SLDQSGKTAL
HFASTLASSD LVSAFIKLGL CSPIRGTTSG RSPLISAILV TNSMERGNFA ELLSALWPNL
WLYDNKNWSF LHHLAFQASK NLESSKFYLR KILEWVIADS GKKQDSLTTL SRELINLQDE
ESGNTCLHLA AESESRWFVN IFLELNADVN LVNKTGVKPA DFDIVKDILT ERKNGAESKS
GTEHDNYILE LVRTSMEFHN KKLESGVNPE SEDEDNTIKE EGSKPKKLAS GSSSSNKIFQ
SIQDLLSNTN HEYDNIIKTK RLQINNLNQS LHDATIVTAN NRFVTNKISE KLAYLDNLKL
QMANISDKLQ LAQKEIPADL KVENENENTK FDSDEPFIIK PIYERLIQGE AADSIKPTDE
ILSQLPPLPI LKARIKAYQE INSKIESELT NLLDYSELTS KFKKVVSFCT GVDINEVDEL
LDGLLEAVEG QQ
//
