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DED1_NEOFI
ID   DED1_NEOFI              Reviewed;         676 AA.
AC   A1CXK7;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=ATP-dependent RNA helicase ded1;
DE            EC=3.6.4.13;
GN   Name=ded1; ORFNames=NFIA_108530;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027685; EAW25359.1; -; Genomic_DNA.
DR   RefSeq; XP_001267256.1; XM_001267255.1.
DR   AlphaFoldDB; A1CXK7; -.
DR   SMR; A1CXK7; -.
DR   STRING; 36630.CADNFIAP00009321; -.
DR   EnsemblFungi; EAW25359; EAW25359; NFIA_108530.
DR   GeneID; 4593848; -.
DR   KEGG; nfi:NFIA_108530; -.
DR   VEuPathDB; FungiDB:NFIA_108530; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   HOGENOM; CLU_003041_16_3_1; -.
DR   OMA; CYRSWVR; -.
DR   OrthoDB; 595675at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
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..676
FT                   /note="ATP-dependent RNA helicase ded1"
FT                   /id="PRO_0000281691"
FT   DOMAIN          221..414
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          425..586
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          655..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           190..218
FT                   /note="Q motif"
FT   MOTIF           358..361
FT                   /note="DEAD box"
FT   COMPBIAS        73..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         234..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   676 AA;  72194 MW;  256CF52083863EC4 CRC64;
     MADSLKMGNL SLNESQHAPA APPSNGRAAY IPPHLRQRTM GANVDGAAAP PPPGPAAGAG
     AWNGPRNAPR GGNWANANAS DFSPRAPNVP NGNNSWTPTE AQRRPFDPHA YGHPGHGGSY
     GGSQGGSAKG SGDGQWRDGK HIPGPANARL ERELFGVPND PTKQSTGINF ANYDDIPVEA
     SGHDVPEPVN AFTNPPLDDH LISNIKLARY QTPTPVQKYS IPIVMNGRDL MACAQTGSGK
     TGGFLFPILS QAFQTGPSAV PAQASGQFGY GRQRKAYPTS LILAPTRELV SQIFDEARKF
     AYRSWVRPCV VYGGADIGSQ LRQIERGCDL LVATPGRLVD LIERGRISLV NIKYLVLDEA
     DRMLDMGFEP QIRRIVEGED MPNVNERQTL MFSATFPRDI QMLARDFLKD YVFLSVGRVG
     STSENITQKV EYVEDHDKRS VLLDILHTHG TSGLTLIFVE TKRMADALSD FLLNQRFPAT
     AIHGDRTQRE RERALEMFRS GRCPILVATA VAARGLDIPN VTHVINYDLP TDIDDYVHRI
     GRTGRAGNTG IATAFFNRGN RGVVRELIDL LKEAHQEVPS FLESIAREGS GYGGRGGRGG
     RGRGGNATRD MRRMGGNVGG GAPSFGGSYG APSGSSYGGG AGGYGAPPAY GGGYGGGYGG
     GSYGNPSGPT GPSSWW
 
 
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