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Database: UniProt
Entry: Q6BXG0
LinkDB: Q6BXG0
Original site: Q6BXG0 
ID   DBP4_DEBHA              Reviewed;         766 AA.
AC   Q6BXG0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   16-OCT-2019, entry version 97.
DE   RecName: Full=ATP-dependent RNA helicase DBP4;
DE            EC=3.6.4.13;
GN   Name=DBP4; OrderedLocusNames=DEHA2B03322g;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
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   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., 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: ATP-dependent RNA helicase required for ribosome
CC       biogenesis. Involved in the release of U14 snoRNA in pre-ribosomal
CC       complexes. Required for pre-rRNA cleavage at site A2 (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Interacts with the U3 and U14 snoRNAs. Associates with
CC       pre-ribosomal complexes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX10/DBP4
CC       subfamily. {ECO:0000305}.
DR   EMBL; CR382134; CAG85100.2; -; Genomic_DNA.
DR   RefSeq; XP_457109.2; XM_457109.1.
DR   SMR; Q6BXG0; -.
DR   STRING; 4959.XP_457109.2; -.
DR   PRIDE; Q6BXG0; -.
DR   EnsemblFungi; CAG85100; CAG85100; DEHA2B03322g.
DR   GeneID; 2913044; -.
DR   KEGG; dha:DEHA2B03322g; -.
DR   InParanoid; Q6BXG0; -.
DR   KO; K14776; -.
DR   OMA; KVRTKYD; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000000599; Chromosome B.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0034512; F:box C/D snoRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008186; F:RNA-dependent ATPase activity; IEA:EnsemblFungi.
DR   GO; GO:0034511; F:U3 snoRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025313; DUF4217.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    766       ATP-dependent RNA helicase DBP4.
FT                                /FTId=PRO_0000232198.
FT   DOMAIN       77    251       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      265    437       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      90     97       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        46     74       Q motif.
FT   MOTIF       199    202       DEAD box.
SQ   SEQUENCE   766 AA;  86824 MW;  3BC6ED32F0C4F268 CRC64;
     MGKKQNNRKV VKSQRKSHRE KEEETLAKLQ ERIDAYDPVV DEKSISQFSD LPISEETARG
     LKEASFASLT DIQKKTIPIS LKGEDVMGTA KTGSGKTLAF LIPTIESLIR NKITEYDGLA
     ALIISPTREL AVQIFEVLVK IGKHNNFSAG LVTGGKDVKY EKERVSKMNI LVGTPGRISQ
     HLNESVGMET SNLQVLVLDE ADRCLDMGFK KQIDNILGHL PPTRQTLLFS ATQSDSVKDL
     ARLSLANPKR VGISSDQELS ATPESLEQYY IKIPLDEKLD VLWSFIKSHL KSKILVFFSS
     SKQVQYAYET FRTLQPGISL LKLYGRHKQT SRMETTMKFS QAQHACLFAT DIVARGLDFP
     AIDWVVQIDC PEDAATYVHR VGRAARFGRA GKSLMMLLPS EENGMLKRLN NNKIELKFMN
     IKQKNKKTIR PQLQSLCFQD PMIKNLGQRA FISYFRSVYV QKDKDIFKID ELPSDKFARS
     LGLPGAPKIK FKGGSDNKEK KNMSRQLAAL SKSNNEGDVV PEEDKKVRTK YDRMFERKNQ
     TILSDHYLNL TGSKADTAEK SDDDDEDFMA VKRQDHELRD DELPDLSIPV SKRSAKKALS
     KKASVAGKGN ANKLKFDDDG VAHAIYELED EEDFKKQGDA RVQKDTFLNK ETELMNNADI
     EDKLTAKEKR QEKKRKRKEM EKNMRQESDD EDENIQTVVS IGGDDIDLDR DLEHSSADED
     VPEPKKPKWF DNDKNVNKDE DDGVVEYDEP QTLEDLEALT SKLLEH
//
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