GenomeNet

Database: UniProt
Entry: A4RHF1
LinkDB: A4RHF1
Original site: A4RHF1 
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   31-JUL-2019, entry version 75.
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
OS   blast fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Magnaporthales; Pyriculariaceae;
OC   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.,
RA   Harding M., Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J.,
RA   Calvo S.E., Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E.,
RA   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
CC       initiation. Remodels RNA in response to ADP and ATP concentrations
CC       by facilitating disruption, but also formation of RNA duplexes (By
CC       similarity). {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
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. {ECO:0000305}.
DR   EMBL; CM001232; EHA55408.1; -; Genomic_DNA.
DR   RefSeq; XP_003715215.1; XM_003715167.1.
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   EuPathDB; FungiDB:MGG_07033; -.
DR   InParanoid; A4RHF1; -.
DR   KO; K11594; -.
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:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   Initiation factor; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome; RNA-binding.
FT   CHAIN         1    671       ATP-dependent RNA helicase DED1.
FT                                /FTId=PRO_0000294612.
FT   DOMAIN      218    411       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      422    584       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     231    238       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       187    215       Q motif.
FT   MOTIF       355    358       DEAD box.
FT   COMPBIAS      9    141       Gly-rich.
FT   COMPBIAS    590    667       Gly-rich.
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
//
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