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Database: UniProt
Entry: Q6BKZ0_DEBHA
LinkDB: Q6BKZ0_DEBHA
Original site: Q6BKZ0_DEBHA 
ID   Q6BKZ0_DEBHA            Unreviewed;      1295 AA.
AC   Q6BKZ0;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   27-MAR-2024, entry version 117.
DE   SubName: Full=DEHA2F17732p {ECO:0000313|EMBL:CAG89514.2};
GN   OrderedLocusNames=DEHA2F17732g {ECO:0000313|EMBL:CAG89514.2};
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:CAG89514.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89514.2, 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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CR382138; CAG89514.2; -; Genomic_DNA.
DR   RefSeq; XP_461131.2; XM_461131.1.
DR   STRING; 284592.Q6BKZ0; -.
DR   GeneID; 2903686; -.
DR   KEGG; dha:DEHA2F17732g; -.
DR   eggNOG; KOG0386; Eukaryota.
DR   HOGENOM; CLU_000315_15_0_1; -.
DR   InParanoid; Q6BKZ0; -.
DR   OMA; VNYISHT; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014012; HSA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029295; SnAC.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF1012; NUCLEAR PROTEIN STH1_NPS1; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07529; HSA; 1.
DR   Pfam; PF14619; SnAC; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM01314; SnAC; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          340..412
FT                   /note="HSA"
FT                   /evidence="ECO:0000259|PROSITE:PS51204"
FT   DOMAIN          522..686
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          833..994
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1211..1281
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1130..1181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1295 AA;  149352 MW;  58458AD50AAEA121 CRC64;
     MSEGPIVTNG NVLHNGSGIG GDISVSRQAI SVSFPETREQ LNALLHKYQQ LMKASNEAKE
     KHDNFVRYLE NKENGVSDFK GTSSDVRPVF KDPTEEERLA IENVFYKISE QYQEFVKNEQ
     TFYESIKAQK SEESLDLELL EKQIAGLQFL SKDLDLPESL QEDYESVINS ESESVRNKDT
     DRFIEAFLRS KSNLNDFMKR AESLGIKVPQ PLGSINPMHA PVGNYYTEQM ISSKISNRIR
     ELENLPANLG TFKTDSLKSQ TNYDDLKIKA LIELKSLQLL AKQKQLKKNL IISQATNSHY
     DNSDLNKVPL TLQARRSIYI RPKIIQPNPH LLASQLEEKR KLEANRIKHA LHVEKVQQIL
     INSEDFVNKK LNRLNKISTI SRAINSFHSV TEKDESKKLE KTAKQRLQAL KANDEEAYIK
     LLDQTKDHRI THLLKQTNTF LDSLAQAVKV QQVEQGADDI SGEKHIENEV VPEKEDNVEE
     LREKIDYYQV AHRVKEEVKE QPSILVGGTL KEYQVKGLEW MVSLYNNKLN GILADEMGLG
     KTIQSISLIT YLIERKHEDK FLVVVPLSTI TNWTMEFEKW APAVDVIVYK GSQQQRKSMQ
     AEVRSGAFQV ILTTYEYIIR ERPLLSKFYY SHMIIDEGHR MKNATSKLSI TLKNYYKTKN
     RLILTGTPLQ NNLPELWALL NFVLPKIFNS VKSFDEWFNT PFANTGSQEK IELTEEESLL
     VIRRLHKVLR PFLLRRLKKD VEKDLPDKVE KVLKCNLSGL QYVLYQQMLK HNALFVGVDV
     GGAKSGIKGL NNKIMQLRKI CNHPFVFEEV ETVLNSTRLT NDLIWRVSGK FELLDRVLPK
     FKASGHRVLI FFQMTQVMNI MEDFLRWRDM KYLRLDGATK AEDRQDMLKD FNAPNSDYFC
     FLLSTRAGGL GLNLQTADTV IIFDTDWNPH QDLQAQDRAH RIGQKNEVRI LRLITNDSVE
     EVILERAHQK LDIDGKVIQA GKFDNKSTSE EQEAFLKRLL EAEASNDDNE ENDSLDDEEL
     NEVLARSEDE KVLFAQIDNE RIINEKLASR QGGPKTRLLE KDELPTVFTE DVSHHFEKDT
     KELARMRDKK RVKYDDGLTE EQWLMAMDND NDTVEDAIRR KEVRVAKRRK NRGGSADLLS
     DDDEDIVDGD LDEENLRPRK RSRRSTTPQA NGYTDNEDDI SELEKVDDSN ELVEKCTIVL
     DELCQLTAEA DGHNISEIFM TLPSRKLYPD YYQVIKQPTS INQIKKNLKQ ENFESFESFM
     DSLQLMCTNA KTYNEEGSWV YEDATTVENF LSSKI
//
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