GenomeNet

Database: UniProt
Entry: Q0CLJ6
LinkDB: Q0CLJ6
Original site: Q0CLJ6 
ID   DED1_ASPTN              Reviewed;         674 AA.
AC   Q0CLJ6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   31-JUL-2019, entry version 70.
DE   RecName: Full=ATP-dependent RNA helicase ded1;
DE            EC=3.6.4.13;
GN   Name=ded1; ORFNames=ATEG_05438;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S.,
RA   White J., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C.,
RA   Denning D.W., Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476600; EAU34507.1; -; Genomic_DNA.
DR   RefSeq; XP_001214616.1; XM_001214616.1.
DR   SMR; Q0CLJ6; -.
DR   STRING; 33178.CADATEAP00005629; -.
DR   PRIDE; Q0CLJ6; -.
DR   EnsemblFungi; EAU34507; EAU34507; ATEG_05438.
DR   GeneID; 4321166; -.
DR   EuPathDB; FungiDB:ATEG_05438; -.
DR   HOGENOM; HOG000268804; -.
DR   OMA; CYRSWVR; -.
DR   OrthoDB; 595675at2759; -.
DR   Proteomes; UP000007963; 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: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    674       ATP-dependent RNA helicase ded1.
FT                                /FTId=PRO_0000281688.
FT   DOMAIN      217    410       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      421    582       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       354    357       DEAD box.
FT   COMPBIAS    585    669       Gly-rich.
SQ   SEQUENCE   674 AA;  71685 MW;  5E16825915D426F5 CRC64;
     MADSLKMGNL SLNESQHAPA PSTASSGRAA YIPPHLRQRQ MGANMDGAAP PPPGPAAAAP
     PQAGGSWGAR PPRGGNWANA NDFSPRGPNG NTSWTPTDGL RRPFNPNAYG NPGHGGGGSS
     SSYARGSGDG QWRDGKHIPG PPNPRVEREL FGLPNDPSKQ STGINFANYD DIPVEASGQD
     VPEPVNAFTN PPLDDHLISN IALARYLTPT PVQKYSIPIV MNGRDLMACA QTGSGKTGGF
     LFPILSQAFQ NGPSPTPAPA GGQLGYGRQR KAYPTSLILA PTRELVSQIF DEARKFAYRS
     WVRPCVVYGG ADIGSQLRQI ERGCDLLVAT PGRLVDLIER GRISLVNIKY LILDEADRML
     DMGFEPQIRR IVEGEDMPHV NDRQTLMFSA TFPRDIQMLA RDFLKDYVFL SVGRVGSTSE
     NITQKVEYVE DHDKRSVLLD ILHTHGTSGL TLIFVETKRM ADSLSDFLLN QRFPATAIHG
     DRTQRERERA LEMFRSGRCP ILVATAVAAS GLDIPNVTHV INYDLPTDID DYVHRIGRTG
     RAGNTGIATA FFNRGNRGVV RDLIDLLKEA HQEVPTFLES IAREGSGYGG RGGRGGRGRG
     GNATRDMRRF GGGGGGMGSA PSYGGGYGGG AGGYSSGGGG SFGGAPSYGG GYGGGYGGGS
     YGNPSGPTGP SSWW
//
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