DED1_ASPNC
ID DED1_ASPNC Reviewed; 678 AA.
AC A2QI25;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=ATP-dependent RNA helicase ded1;
DE EC=3.6.4.13;
GN Name=ded1; ORFNames=An04g02030;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270071; CAL00690.1; -; Genomic_DNA.
DR RefSeq; XP_001401571.1; XM_001401534.1.
DR AlphaFoldDB; A2QI25; -.
DR SMR; A2QI25; -.
DR PaxDb; A2QI25; -.
DR EnsemblFungi; CAL00690; CAL00690; An04g02030.
DR GeneID; 4990608; -.
DR KEGG; ang:ANI_1_430184; -.
DR VEuPathDB; FungiDB:An04g02030; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR Proteomes; UP000006706; Chromosome 6L.
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 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..678
FT /note="ATP-dependent RNA helicase ded1"
FT /id="PRO_0000281687"
FT DOMAIN 218..411
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 422..583
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..678
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 85..100
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 678 AA; 72132 MW; E8E4794D93C1E227 CRC64;
MADSLKMGNL SLNESQHAPA PAPSTGRAAY IPPHLRGRQM GGNMDGAAAA APPPGPAAGP
GNSWGGPRGG PRGGQWANAN APDFSPRGPN GNTSWSPHEA RRPFNPNAYG HPGHGGSYGS
GGGSARGSGD GQWRDGKHIP GPANPRLERE LFGLPNDPTK QNTGINFANY DDIPVEASGH
DVPEPVNAFT NPPLDDHLIE NIKLAHYQTP TPVQKYSIPI VMNGRDLMAC AQTGSGKTGG
FLFPILSQAY QNGPSAAPAQ AGGQFGYGRQ RKAYPTSLIL APTRELVSQI FDEARKFAYR
SWVRPCVVYG GADIGSQLRQ IERGCDLLVA TPGRLVDLIE RGRISLVNIK YLILDEADRM
LDMGFEPQIR RIVEGEDMPH VNDRQTLMFS ATFPRDIQML ARDFLKDYVF LSVGRVGSTS
ENITQKVEYV EDHDKRSVLL DILHTHGTSG LTLIFVETKR MADSLSDFLL NQRFPATAIH
GDRTQRERER ALEMFRSGRC PILVATAVAA RGLDIPNVTH VINYDLPTDI DDYVHRIGRT
GRAGNTGIAT AFFNRGNRGV VRDLIDLLKE AHQEVPSFLE SIAREGSGYG GRGGRGGRGR
GANATRDMRR MGGGMGGPPS FGGSSYGAPG GSYGGGGGGS SSYGAPPSYG GGGGYGGGGS
YGGGYGNPSG PTGPSSWW
