GenomeNet

Database: UniProt
Entry: A6SEH9
LinkDB: A6SEH9
Original site: A6SEH9 
ID   DED1_BOTFB              Reviewed;         683 AA.
AC   A6SEH9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   31-JUL-2019, entry version 69.
DE   RecName: Full=ATP-dependent RNA helicase ded1;
DE            EC=3.6.4.13;
GN   Name=ded1; ORFNames=BC1G_10862;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P.,
RA   Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S.,
RA   Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M.,
RA   Pradier J.-M., Quevillon E., Sharon A., Simon A., ten Have A.,
RA   Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V.,
RA   Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z.,
RA   Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C.,
RA   Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S.,
RA   Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M.,
RA   Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C.,
RA   Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H.,
RA   Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C.,
RA   Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476921; EDN32334.1; -; Genomic_DNA.
DR   RefSeq; XP_001550389.1; XM_001550339.1.
DR   SMR; A6SEH9; -.
DR   PRIDE; A6SEH9; -.
DR   GeneID; 5430884; -.
DR   KEGG; bfu:BCIN_05g00090; -.
DR   EuPathDB; FungiDB:Bcin05g00090; -.
DR   KO; K11594; -.
DR   OMA; CYRSWVR; -.
DR   OrthoDB; 595675at2759; -.
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; Cytoplasm; Helicase; Hydrolase; Initiation factor;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding.
FT   CHAIN         1    683       ATP-dependent RNA helicase ded1.
FT                                /FTId=PRO_0000310181.
FT   DOMAIN      217    408       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      419    579       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     230    237       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       186    214       Q motif.
FT   MOTIF       352    355       DEAD box.
FT   COMPBIAS     27    140       Gly-rich.
FT   COMPBIAS    582    679       Gly-rich.
SQ   SEQUENCE   683 AA;  71555 MW;  9CB31041B9B42759 CRC64;
     MADQLNMNGL NLNGGEPRSY IPPHMRGKMG GPAPAGPPAN LNGSAWAPQG NGYANGPRPA
     GGDSWANAPD FTPRGNGAPR GGNNWNPSGP PSFNKNAYGN PAAGAGGPGG AGGAGGAGGG
     AGQARGGGDG QWRDGKHIAG PANARVEREL FGIADDPTKQ QTGINFEKYD DIPVEASGQD
     VPEPVLKFTN PPLDDHLIKN IELAHYKVPT PVQKYSIPIV MGGRDLMACA QTGSGKTGGF
     LFPILSQAFQ TGPSPVPANA AGSFGRTRKA YPTSLILAPT RELVSQIYDE SRKFAYRSWV
     RPCVVYGGAD IGSQLRQMER GCDLLVATPG RLVDLIERGR ISLQNIKYLV LDEADRMLDM
     GFEPQIRRIV EGEDMPGVQN RQTLMFSATF PRDIQMLARD FLKDYVFLSV GRVGSTSENI
     TQKVEYVEDI DKRSVLLDIL HTHGAGLTLI FVETKRMADS LSDFLINQNF PATSIHGDRT
     QRERERALEM FRNGRCPILV ATAVAARGLD IPNVKHVVNY DLPTDIDDYV HRIGRTGRAG
     NTGISTAFFN RGNRGVCRDL IELLKEANQE IPSFLENIAR EGGGFGGGRG GRSGGRGRGG
     GANRDFRKFG GGGGGGFNGG GGFGGPPASG GYGGGGGGFG GPPAPSSYGP PPGQYGGGGG
     GYGGGNGGGY GNPSAGGGGQ SWW
//
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