ID Q6BJE1_DEBHA Unreviewed; 1590 AA.
AC Q6BJE1;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 125.
DE SubName: Full=DEHA2G03102p {ECO:0000313|EMBL:CAG90128.2};
GN OrderedLocusNames=DEHA2G03102g {ECO:0000313|EMBL:CAG90128.2};
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:CAG90128.2, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG90128.2, 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; CR382139; CAG90128.2; -; Genomic_DNA.
DR RefSeq; XP_461680.2; XM_461680.1.
DR STRING; 284592.Q6BJE1; -.
DR GeneID; 2904548; -.
DR KEGG; dha:DEHA2G03102g; -.
DR VEuPathDB; FungiDB:DEHA2G03102g; -.
DR eggNOG; KOG0386; Eukaryota.
DR HOGENOM; CLU_000315_15_1_1; -.
DR InParanoid; Q6BJE1; -.
DR OMA; NPTRETN; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000000599; Chromosome G.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05519; Bromo_SNF2; 1.
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; IPR018359; Bromodomain_CS.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
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:SF973; ATP-DEPENDENT HELICASE BRM; 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; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
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.
DR PROSITE; PS51666; QLQ; 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 173..213
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 530..603
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 708..873
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1021..1184
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1431..1501
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 49..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1590 AA; 181860 MW; 0DDC031008CF8FDF CRC64;
MNRQFSREEI QKILQRWHQL RQQFGDQAIN VPEFTHLSKI IKYLQQQNQQ SLQRKTTPQD
TTQPHTQQQI PQQQQQQFQA SPQVAQPINS SNGTPSVPNA MMGQVPGNIG GNTQRTVSQQ
QYQPPQQSTF TPQTQAPQVV PQQQMPFQNG APVNSNNIPP TMQNNVNNSS ESAFSAQQVQ
MLKVQFQAFK FLLKSPGPGS PLIPQNVIDF VTNDRLAFAN GNYLPSTGQQ PVINTQTPQF
AQSQLPGQSR HPSQTQSSLG PNLQSPMMPM QPNMPQVNKP IPANNIPFTT SQEDLSNGLK
KQNRRGPKPK MLNQGINSNT ISIANQVPGQ QIPKRQPSIK PSTRDRSLTP STNNSYNPVC
LEPKPPVNID ELVPDRATTT KTIVPINRPN VQVDCFEVPD ILSDKFKDIP YTALYTIQSR
FQIPGLLPEG IDMDNIVNNR EALIVLQIDQ KITYLRKQLN ESDNEDESNQ IKAEISKLEL
LPYQKELRGK ILSQAWFSKS LLPNSHPNFL AKFNNLSSDN VISTHELYKQ QLHSLVQAQN
KKHQGTIKEI LSAKATRNRR QFSKKEKIER FANKISSFHS QTAKEEQKKL EKMAKQRLQA
LKSNDEEAYL KLLDHTKDTR ITHLLKQTNQ FLDSLAQAVQ SQQQESHDRV QRAVPDNNVD
VSNDEEKREK MDYYHVAHRI KEEVTKQPSI LVGGTLKEYQ IKGLQWMVSL FNNHLNGILA
DEMGLGKTIQ TISLLTYLIE IKKISGPFLV IVPLSTLTNW NIEFEKWAPG VKKITYKGTP
TQRKVLQHDV KSGNFQILLT TFEYIIKDRN LLSKVKWVHM IIDEGHRMKN ANSKLSETLT
HHYHSDYRLI LTGTPLQNNL PELWALLNFV LPKIFNSVKS FDEWFNTPFA NTGGQDKIEL
SEEETLLVIR RLHKVLRPFL LRRLKKDVEK DLPNKVEKVV KCKMSSLQSK LYQQMLKYNI
LYASKPGEGD KPVLIKNANN QIMQLRKICN HPFVYEEVEN LINPASETND QIWRVAGKFE
LLDKVLPKFK NSGHRVLIFF QMTQIMDIME DFLRLRGMKY MRLDGSTKAD DRTGLLKLFN
APNSDYFCFL LSTRAGGLGL NLQTADTVII FDTDWNPHQD LQAQDRAHRI GQKNEVRILR
LITEDSVEEM ILERAHAKLE IDGKVIQAGK FDNKSTAEEQ EALLRALLEK EDERKQKGIV
DDNDDLDDDE LNQVIARNDD ELIAFRKLDE ERSIETKEAS YPSRLYTDQE LPEIYQKDPE
VILKKDEVIE EYGRGNRERR TALYDDNLTE EQWLKTIEGV VSDDSDGERD SKPKRARGRP
RGMPRSNDDT DMDENGEFRS QTDSVSSKKR KAFIDDDLSD DSSAKRQRQT TPKASVPRGR
GRGRGRGGRG RGSLLYRATP AVDPLSPDER QTLQGNMITI YDSIINHADD QGRILSDLFL
QKPSKKLYPD YYVLIKHPIA LDIIKKRIQG RSYTNIREIL EDFHLMFSNA RIYNEEGSIV
YQDAVALEDL VVEKFEELNS HLEPEVIKKT LDFTDFDEIF NLKPLSSNSA VKQPIDRKVE
ELDADESFES PISTSGADGL DFDETPLDIN
//
