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   03-AUG-2022, entry version 116.
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 Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   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 Saccharomyces
RT   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 pore
CC       complex and essential for mRNA export from the nucleus. May participate
CC       in a terminal step of mRNA export through the removal of proteins that
CC       accompany mRNA through the nucleopore complex. May also be involved in
CC       early transcription (By 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: Associates with the nuclear pore complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore
CC       complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore
CC       complex cytoplasmic fibrils. {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE016816; AAS51304.2; -; Genomic_DNA.
DR   RefSeq; NP_983480.2; NM_208833.2.
DR   AlphaFoldDB; Q75C39; -.
DR   SMR; Q75C39; -.
DR   STRING; 33169.AAS51304; -.
DR   EnsemblFungi; AAS51304; AAS51304; AGOS_ACR078W.
DR   GeneID; 4619605; -.
DR   KEGG; ago:AGOS_ACR078W; -.
DR   eggNOG; KOG0332; Eukaryota.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; Q75C39; -.
DR   OMA; EYCTPIQ; -.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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; IBA:GO_Central.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006415; P:translational termination; IEA:EnsemblFungi.
DR   GO; GO:0006409; P:tRNA export from nucleus; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.300; -; 2.
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; Cytoplasm; Helicase; Hydrolase; Membrane; mRNA transport;
KW   Nuclear pore complex; Nucleotide-binding; Nucleus; Protein transport;
KW   Reference proteome; RNA-binding; Translocation; Transport.
FT   CHAIN           1..466
FT                   /note="ATP-dependent RNA helicase DBP5"
FT                   /id="PRO_0000227947"
FT   DOMAIN          110..277
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          288..465
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           77..105
FT                   /note="Q motif"
FT   MOTIF           224..227
FT                   /note="DEAD box"
FT   COMPBIAS        14..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         123..130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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