GenomeNet

Database: UniProt
Entry: Q1DJF0
LinkDB: Q1DJF0
Original site: Q1DJF0 
ID   DED1_COCIM              Reviewed;         665 AA.
AC   Q1DJF0; A0A0D6K9M7; J3K0D9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   31-JUL-2019, entry version 74.
DE   RecName: Full=ATP-dependent RNA helicase DED1;
DE            EC=3.6.4.13;
GN   Name=DED1; ORFNames=CIMG_09563;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J.,
RA   Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E.,
RA   Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M.,
RA   Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N., Orbach M.J.,
RA   Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens
RT   Coccidioides and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704915; EAS28359.2; -; Genomic_DNA.
DR   RefSeq; XP_001239942.2; XM_001239941.2.
DR   SMR; Q1DJF0; -.
DR   PRIDE; Q1DJF0; -.
DR   EnsemblFungi; EAS28359; EAS28359; CIMG_09563.
DR   GeneID; 4558926; -.
DR   KEGG; cim:CIMG_09563; -.
DR   EuPathDB; FungiDB:CIMG_09563; -.
DR   eggNOG; KOG0335; Eukaryota.
DR   eggNOG; ENOG410XNTI; LUCA.
DR   InParanoid; Q1DJF0; -.
DR   KO; K11594; -.
DR   OMA; CYRSWVR; -.
DR   OrthoDB; 595675at2759; -.
DR   Proteomes; UP000001261; 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    665       ATP-dependent RNA helicase DED1.
FT                                /FTId=PRO_0000255986.
FT   DOMAIN      212    405       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      416    576       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     225    232       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       181    209       Q motif.
FT   MOTIF       349    352       DEAD box.
FT   COMPBIAS     59    135       Gly-rich.
FT   COMPBIAS    579    660       Gly-rich.
SQ   SEQUENCE   665 AA;  71139 MW;  513D5C022649C51F CRC64;
     MADSLKMAGL SLEDSQHAPS HATGRAPYIP PHLRGQQRAG PTMPVDGAAP QGRPPMNPGS
     WGPNGAPPNN WAPRGANNIN GAPAWGAAGG GGARFDPNAY GHPGHRGGQS HGGAGSGAAR
     GSGDGQWRDG KHIPGPPNAR LERELFGVPN DPSKQHTGIN FANYDDIPVE ASGHDVPEPV
     TTFTNPPLDD HLISNIKLAT YKTPTPVQKY SIPIVMGGRD LMACAQTGSG KTGGFLFPIL
     SQAFKNGPSA VPTQNANQFS YGRQRKAYPT SLILAPTREL VSQIYDEARK FAYRSWVRPC
     VVYGGADIGS QLRQIERGCD LLVATPGRLV DLIERGRISL CNIKYLVLDE ADRMLDMGFE
     PQIRRIVEGE DMPPVNGRQT LMFSATFPRD IQMLARDFLK DYVFLSVGRV GSTSENITQK
     VEYVEDADKR SVLLDILHTH GTGLTLIFVE TKRMADSLSE FLINQNFPAT AIHGDRTQRE
     RERALEYFRN GRCPILVATA VAARGLDIPN VTHVVNYDLP TDIDDYVHRI GRTGRAGNTG
     LSTAFFNRGN RGVVRDLIEL LKEAHQEVPA FLENIAREGS GYGGRGGGRG GGRGRGANAT
     RDMRRMGGGG PPMSGTPSYS GGYGGGANNY GGSYSSAPSY GGYGGGYGGG SYGNPSGPTG
     PSSWW
//
DBGET integrated database retrieval system