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 13-NOV-2013, entry version 72. 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 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 SEQUENCE REVISION TO 590 AND 598. RA Dietrich F.S., Voegeli S., Philippsen P.; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ATP-binding RNA helicase involved in translation CC initiation. Remodels RNA in response to ADP and ATP concentrations CC by facilitating disruption, but also formation of RNA duplexes (By CC similarity). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). 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. DDX3/DED1 CC subfamily. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. 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 STRING; 33169.AGOS_ADL273C; -. DR PRIDE; Q75B50; -. DR GeneID; 4619958; -. DR KEGG; ago:AGOS_ADL273C; -. DR eggNOG; COG0513; -. DR HOGENOM; HOG000268804; -. DR KO; K11594; -. DR OrthoDB; EOG7TJ3T2; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. DR InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N. 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 Initiation factor; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; RNA-binding. FT CHAIN 1 623 ATP-dependent RNA helicase DED1. FT /FTId=PRO_0000227953. FT DOMAIN 177 365 Helicase ATP-binding. FT DOMAIN 392 536 Helicase C-terminal. FT NP_BIND 190 197 ATP (By similarity). FT MOTIF 146 174 Q motif. FT MOTIF 309 312 DEAD box. 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 //