GenomeNet

Database: UniProt
Entry: Q6FKN8
LinkDB: Q6FKN8
Original site: Q6FKN8 
ID   DBP5_CANGA              Reviewed;         504 AA.
AC   Q6FKN8;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   13-NOV-2019, entry version 108.
DE   RecName: Full=ATP-dependent RNA helicase DBP5;
DE            EC=3.6.4.13;
GN   Name=DBP5; OrderedLocusNames=CAGL0L10021g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380958; CAG62178.1; -; Genomic_DNA.
DR   RefSeq; XP_449206.1; XM_449206.1.
DR   SMR; Q6FKN8; -.
DR   STRING; 5478.XP_449206.1; -.
DR   PRIDE; Q6FKN8; -.
DR   EnsemblFungi; CAG62178; CAG62178; CAGL0L10021g.
DR   GeneID; 2891053; -.
DR   KEGG; cgr:CAGL0L10021g; -.
DR   CGD; CAL0135432; CAGL0L10021g.
DR   EuPathDB; FungiDB:CAGL0L10021g; -.
DR   eggNOG; KOG0332; Eukaryota.
DR   eggNOG; ENOG410XRGX; LUCA.
DR   InParanoid; Q6FKN8; -.
DR   KO; K18655; -.
DR   OMA; CKLYGLM; -.
DR   Proteomes; UP000002428; Chromosome L.
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   GO; GO:0006409; P:tRNA export from nucleus; 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    504       ATP-dependent RNA helicase DBP5.
FT                                /FTId=PRO_0000232220.
FT   DOMAIN      147    314       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      325    502       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     160    167       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       114    142       Q motif.
FT   MOTIF       261    264       DEAD box.
SQ   SEQUENCE   504 AA;  56684 MW;  4B1272E2CA59C9FB CRC64;
     MSATEDKKDP ASMLAELKLD KDEGNKTPET KTPESNSAET KTTEEVKELK NPFTQKKEDV
     ENDAAEEKTN EVNKDDAKDE RENKDTNLIK SEYEVKVNLA DLQADPNSPL YSVKSFDELG
     LSPELLKGIY AMKFQKPSKI QERALPLLLS NPPRNMIAQS QSGTGKTAAF SLTMLSRVDE
     TQNVPQAICL APSRELARQT LEVIQEMGKY TKITTQLIVP DSFEKNTKIN ANVVVGTPGT
     LLDLIRRKLI QLQNVKIFVL DEADNMLDKQ GLGDQCIRVK KFLPKDTQLV LFSATFADAV
     KAYAQKVIPN ANTLELQRNE VNVKAIKQLY MDCNDEAHKY EVLCELYGLL TIGSSIIFVA
     KKDTANLLYG KLKHEGHQVS ILHSDLRTDE RDRLIDDFRE GRSKVLITTN VLARGIDIPS
     VSMVVNYDLP TLPNGMPDYA TYVHRIGRTG RFGRTGVAIS FVHDKKSFKI LSAIQDYFKD
     IELTRVPTDD WDEVEDIVKK VLKQ
//
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