DED1_ASHGO
ID DED1_ASHGO Reviewed; 623 AA.
AC Q75B50;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=ATP-dependent RNA helicase DED1;
DE EC=3.6.4.13;
GN Name=DED1; OrderedLocusNames=ADL273C;
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 590 AND 598.
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-binding RNA helicase involved in translation initiation.
CC Remodels RNA in response to ADP and ATP concentrations by facilitating
CC disruption, but also formation of RNA duplexes (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 -!- SUBCELLULAR LOCATION: Cytoplasm {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. DDX3/DED1
CC subfamily. {ECO:0000305}.
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DR EMBL; AE016817; AAS51647.2; -; Genomic_DNA.
DR RefSeq; NP_983823.2; NM_209176.2.
DR AlphaFoldDB; Q75B50; -.
DR SMR; Q75B50; -.
DR STRING; 33169.AAS51647; -.
DR PRIDE; Q75B50; -.
DR EnsemblFungi; AAS51647; AAS51647; AGOS_ADL273C.
DR GeneID; 4619958; -.
DR KEGG; ago:AGOS_ADL273C; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; Q75B50; -.
DR OMA; CYRSWVR; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0031370; F:eukaryotic initiation factor 4G binding; IEA:EnsemblFungi.
DR GO; GO:0003729; F:mRNA 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:0033592; F:RNA strand annealing activity; IEA:EnsemblFungi.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:1901195; P:positive regulation of formation of translation preinitiation complex; IEA:EnsemblFungi.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IEA:EnsemblFungi.
DR CDD; cd17967; DEADc_DDX3_DDX4; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044763; Ded1/Dbp1_DEADc.
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; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..623
FT /note="ATP-dependent RNA helicase DED1"
FT /id="PRO_0000227953"
FT DOMAIN 177..365
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 392..536
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 146..174
FT /note="Q motif"
FT MOTIF 309..312
FT /note="DEAD box"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 190..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 623 AA; 67549 MW; 066FD8BA4FA91CAB CRC64;
MSELVNKMEN LSVGDSAQKK SAYVPPHVKR RMKEGGSEPS SRNTENFGNG GRFGGSEHNG
FGGGRGSWFG GNARGGGPRS SDRGGSSRFG KWVDGKHVPM KRNEKLEVQL FGTPEDPNFQ
SSGINFDNYD DIPVDASGED VPDPITEFTS PPLDELLLEN IKLARFTKPT PVQKYSVPIV
AKGRDLMACA QTGSGKTGGF LFPVLSQSFS NGPASTPDES GYYMRKAYPT AVVLAPTREL
ATQIFDEAKK FTYRSWVKPC VVYGGADIRQ QIRELERGCD LIVATPGRLN DLLERGKISL
CSVKYLVLDE ADRMLDMGFE PQIRHIVEGC DMPTVENRQT LMFSATFPTD IQHLAADFLK
DYIFLSVGRV GSTSENITQK VLHVEDIDKR SVLLDLLAAS DGGLTLVFVE TKRMADALTD
FLIMQNLSAT AIHGDRTQAE RERALAFFRT GRANVLVATA VAARGLDIPN VTHVINYDLP
SDIDDYVHRI GRTGRAGNTG LATAFFNRGN KNVVKELVDI LEEANQEVPS FLSQIAKEMS
YGGGGGKSSR GGRGGYSRGN STRDFRRHGG GGGSEWSSAN RASSGWGNAN RTGSGWGGSS
GFGGSTESWS NASKTVGSNN SWW
