DED1_MAGO7
ID DED1_MAGO7 Reviewed; 671 AA.
AC A4RHF1; G4MZP4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=ATP-dependent RNA helicase DED1;
DE EC=3.6.4.13;
GN Name=DED1; ORFNames=MGG_07033;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; CM001232; EHA55408.1; -; Genomic_DNA.
DR RefSeq; XP_003715215.1; XM_003715167.1.
DR AlphaFoldDB; A4RHF1; -.
DR SMR; A4RHF1; -.
DR STRING; 318829.MGG_07033T0; -.
DR PRIDE; A4RHF1; -.
DR EnsemblFungi; MGG_07033T0; MGG_07033T0; MGG_07033.
DR GeneID; 2683047; -.
DR KEGG; mgr:MGG_07033; -.
DR VEuPathDB; FungiDB:MGG_07033; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; A4RHF1; -.
DR OMA; CYRSWVR; -.
DR OrthoDB; 595675at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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:0031047; P:gene silencing by RNA; IEA:EnsemblFungi.
DR GO; GO:1990625; P:negative regulation of cytoplasmic translational initiation in response to stress; 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; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..671
FT /note="ATP-dependent RNA helicase DED1"
FT /id="PRO_0000294612"
FT DOMAIN 218..411
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 422..584
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 187..215
FT /note="Q motif"
FT MOTIF 355..358
FT /note="DEAD box"
FT COMPBIAS 59..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 231..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 671 AA; 70694 MW; AA423E509B95D2F9 CRC64;
MADQLNMAGL SVGGGGPGNG PRSYIPPHMR GKVGGPGMNG PQNGPQNGGG PPGHDGPPSS
VNNGLNNSAW AGNQNHDARG GNWGNQGGGP PPRNNNWNRP SFNPNAYGGG NQGGGHGGGG
GGGYARGSGD GQWRDGKHIP GPVNARVERE LFGTPDDPSK QHTGINFEKY DDIPVEASGH
DVPEPVYTFS NPPLDDHLIS NIELARYKVP TPVQKYSVPI VMGGRDLMAC AQTGSGKTGG
FLFPILSQAF KTGPSPIPAT NQGPGGYGRQ RKAYPTSLIL APTRELVSQI YDESRKFAYR
SWVRPCVVYG GADIGSQLRQ IERGCDLLVA TPGRLVDLIE RGRISLCNIK YLVLDEADRM
LDMGFEPQIR RIVEGEDMPN VQDRQTLMFS ATFPGYIQQL ARDFLKDYIF LSVGRVGSTS
ENITQRVMEV KHRDDKISHL LDLLSTHGGG LTLIFVETKR NADELSDFLQ NQNLPATSIH
GDRTQRERER ALEMFRTGRC PILVATAVAA RGLDIPNVTH VINYDLPTDI DDYVHRIGRT
GRAGNTGIAT AFFDMKDNSG VAQELLNILK EAKQDIPPFL ETAARMKSYG GGRGRGGGGR
GRGGGGNRDF RKFGGGGGGG FNGGGGGGFS GGGYGGGGGG YGGGGGGYGG GGYGGGGGGS
YGNPGGGQSW W
