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Database: UniProt
Entry: Q75C39
LinkDB: Q75C39
Original site: Q75C39 
ID   DBP5_ASHGO              Reviewed;         466 AA.
AC   Q75C39;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   13-NOV-2019, entry version 107.
DE   RecName: Full=ATP-dependent RNA helicase DBP5;
DE            EC=3.6.4.13;
GN   Name=DBP5; OrderedLocusNames=ACR078W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient
RT   Saccharomyces cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO N-TERMINUS; 113 AND 158.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016816; AAS51304.2; -; Genomic_DNA.
DR   RefSeq; NP_983480.2; NM_208833.2.
DR   SMR; Q75C39; -.
DR   STRING; 33169.AAS51304; -.
DR   EnsemblFungi; AAS51304; AAS51304; AGOS_ACR078W.
DR   GeneID; 4619605; -.
DR   KEGG; ago:AGOS_ACR078W; -.
DR   HOGENOM; HOG000268797; -.
DR   InParanoid; Q75C39; -.
DR   KO; K18655; -.
DR   OMA; CKLYGLM; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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    466       ATP-dependent RNA helicase DBP5.
FT                                /FTId=PRO_0000227947.
FT   DOMAIN      110    277       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      288    465       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     123    130       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        77    105       Q motif.
FT   MOTIF       224    227       DEAD box.
SQ   SEQUENCE   466 AA;  51664 MW;  E8181F78D9AEF5D3 CRC64;
     MSGNAQKPDA SEMLADLDLN KKTKETTLEA GSAESAPSAP AENQAKSDSN LINSEYEVKV
     RLADIQADPN SPLYSVKSFE ELGLAPELLK GLYAMKFQKP SKIQERALPL LLHNPPRNMI
     AQSQSGTGKT AAFSLTMLSR VDVAVPATQA ICLAPSRELA RQTLEVIQEM GKFTKIASQL
     IVPDSYEKNK AINAHIIVGT PGTVLDLMRR KMIQLGKVKT FVLDEADNML DKQGLGDQCI
     RVKKFLPKDT QLVLFSATFD DSVREYARRV VPNANSLELQ RNEVNVSAIK QLFMDCNDER
     HKFTVLCDLY GLLTIGSSII FVQTKQTANM LYTELKREGH QVSILHGDLQ SADRDRLIGD
     FREGRSKVLI TTNVLARGID IPTVSMVVNY DLPMTANGQP DPSTYVHRIG RTGRFGRTGV
     AISFIHDKKS YETLAAIQSY FGDIQITKVP TDDMDEMEKI VKKVLK
//
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