ID DED1_EREGS Reviewed; 623 AA. AC Q75B50; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2013, sequence version 2. DT 24-JAN-2024, entry version 115. DE RecName: Full=ATP-dependent RNA helicase DED1; DE EC=3.6.4.13; GN Name=DED1; OrderedLocusNames=ADL273C; OS Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL OS Y-1056) (Yeast) (Ashbya 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE016817; AAS51647.2; -; Genomic_DNA. DR RefSeq; NP_983823.2; NM_209176.2. DR AlphaFoldDB; Q75B50; -. DR SMR; Q75B50; -. DR STRING; 284811.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; MFRNGRC; -. DR OrthoDB; 5480645at2759; -. 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:0002183; P:cytoplasmic translational initiation; IEA:EnsemblFungi. DR GO; GO:1990625; P:negative regulation of cytoplasmic translational initiation in response to stress; IEA:EnsemblFungi. DR GO; GO:1901195; P:positive regulation of formation of translation preinitiation complex; IEA:EnsemblFungi. DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:EnsemblFungi. DR GO; GO:0000390; P:spliceosomal complex disassembly; IEA:EnsemblFungi. DR CDD; cd17967; DEADc_DDX3_DDX4; 1. DR CDD; cd18787; SF2_C_DEAD; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1. DR PANTHER; PTHR47958:SF32; RNA HELICASE; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 //