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Database: UniProt
Entry: Q6CJU1
LinkDB: Q6CJU1
Original site: Q6CJU1 
ID   DBP5_KLULA              Reviewed;         469 AA.
AC   Q6CJU1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   16-OCT-2019, entry version 106.
DE   RecName: Full=ATP-dependent RNA helicase DBP5;
DE            EC=3.6.4.13;
GN   Name=DBP5; OrderedLocusNames=KLLA0F15950g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
OS   1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37;
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 associated with the nuclear
CC       pore complex and essential for mRNA export from the nucleus. May
CC       participate in a terminal step of mRNA export through the removal
CC       of proteins that accompany mRNA through the nucleopore complex.
CC       May also be involved in early transcription (By similarity).
CC       {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: Associates with the nuclear pore complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nuclear
CC       pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC       Note=Nuclear pore complex cytoplasmic fibrils. {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. DDX19/DBP5
CC       subfamily. {ECO:0000305}.
DR   EMBL; CR382126; CAG98506.1; -; Genomic_DNA.
DR   RefSeq; XP_455798.1; XM_455798.1.
DR   SMR; Q6CJU1; -.
DR   STRING; 28985.XP_455798.1; -.
DR   PRIDE; Q6CJU1; -.
DR   EnsemblFungi; CAG98506; CAG98506; KLLA0_F15950g.
DR   GeneID; 2895852; -.
DR   KEGG; kla:KLLA0_F15950g; -.
DR   eggNOG; KOG0332; Eukaryota.
DR   eggNOG; ENOG410XRGX; LUCA.
DR   HOGENOM; HOG000268797; -.
DR   InParanoid; Q6CJU1; -.
DR   KO; K18655; -.
DR   OMA; CKLYGLM; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IEA:EnsemblFungi.
DR   GO; GO:0005844; C:polysome; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000822; F:inositol hexakisphosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0016973; P:poly(A)+ mRNA export from nucleus; IEA:EnsemblFungi.
DR   GO; GO:0006415; P:translational termination; IEA:EnsemblFungi.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
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; Cytoplasm; Helicase; Hydrolase;
KW   Membrane; mRNA transport; Nuclear pore complex; Nucleotide-binding;
KW   Nucleus; Protein transport; Reference proteome; RNA-binding;
KW   Translocation; Transport.
FT   CHAIN         1    469       ATP-dependent RNA helicase DBP5.
FT                                /FTId=PRO_0000232225.
FT   DOMAIN      112    279       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      290    459       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     125    132       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        79    107       Q motif.
FT   MOTIF       226    229       DEAD box.
SQ   SEQUENCE   469 AA;  52126 MW;  F57062F8DAF06774 CRC64;
     MAQLSKEASD LMARLNIKEP AKKASEDNDT TSETKVEKED AKETKAEEPA NKVINSEYEV
     KVNLADLQAD ANSPLYSVKS FEELGLSEEL LKGLYAMKFQ KPSKIQEKAL PLLIRDPPHN
     MIAQSQSGTG KTAAFSLTML TRVDPNVNST QAICLSPARE LARQTLEVIQ EMGKFTKTSS
     QLVVPDSFER NKPITANIVV GTPGTVLDLI RRKMLNLGSI KVFVLDEADN MLDKQGLGDQ
     CIRVKKFLPK TCQLVLFSAT FDDGVRQYAK KIIPTAVSLE LQKNEVNVSA IKQLFMDCDN
     EEHKYTILSE LYGLLTIGSS IIFVKTKQTA NLLYAKLKKE GHQVSILHGD LQSQDRDRLI
     DDFREGRSKV LITTNVLARG IDIPSVSMVV NYDLPTLPNG QADPSTYVHR IGRTGRFGRT
     GVAISFIHDK KSFEVLSAIQ KYFGDIEITK VPTDDLDEME TIVKKALKA
//
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