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Database: UniProt
Entry: Q0UWA6
LinkDB: Q0UWA6
Original site: Q0UWA6 
ID   DED1_PHANO              Reviewed;         696 AA.
AC   Q0UWA6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-OCT-2019, entry version 75.
DE   RecName: Full=ATP-dependent RNA helicase DED1;
DE            EC=3.6.4.13;
GN   Name=DED1; ORFNames=SNOG_03958;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173)
OS   (Glume blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Phaeosphaeriaceae; Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing
RT   and EST analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAT89163.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; CH445329; EAT89163.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001794501.1; XM_001794449.1.
DR   SMR; Q0UWA6; -.
DR   STRING; 13684.SNOT_03958; -.
DR   PRIDE; Q0UWA6; -.
DR   GeneID; 5971364; -.
DR   KEGG; pno:SNOG_03958; -.
DR   InParanoid; Q0UWA6; -.
DR   KO; K11594; -.
DR   OMA; CYRSWVR; -.
DR   OrthoDB; 595675at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0043186; C:P granule; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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    696       ATP-dependent RNA helicase DED1.
FT                                /FTId=PRO_0000255987.
FT   DOMAIN      232    423       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      434    594       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     245    252       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       201    229       Q motif.
FT   MOTIF       367    370       DEAD box.
FT   COMPBIAS     55    155       Gly-rich.
FT   COMPBIAS    597    692       Gly-rich.
SQ   SEQUENCE   696 AA;  72492 MW;  3F40607DE5CB0807 CRC64;
     MAEQLDMGRL NLNDSQHAPQ NGFNGERSAY IPPHLRGRPQ GGPPPMNAAP PMMNGGGGVG
     GSAWGPAPGG PSPAPPARFD GPPPGQMNGG GNWANANAQA FTPRGRDGPQ GGGGWGGAAP
     GKFDPSAYGK PGGGGGGSAR GSGDGQWKDG KHVPGPSNPR VERELFGVPN DPSKQQTGIN
     FEKYDDIPVE ASGQGVPEPV TRFTNPPLDD HLLSNIELSG YKVPTPVQKY SIPIVMGGRD
     LMACAQTGSG KTGGFLFPIL AQAFQNGPSP PPTAQAGGYG RQRKAYPTSL ILAPTRELVS
     QIFDEARKFA YRSWVRPCVV YGGADIGSQL RQIERGCDLL VATPGRLVDL IERGRISLAS
     IKYLVLDEAD RMLDMGFEPQ IRRIVEGEDM PPTAGRQTLM FSATFPRDIQ MLARDFLKEY
     IFLSVGRVGS TSENITQKIE YVEDADKRSV LLDILHTHGA GLSLIFVETK RMADSLSDFL
     INQGFPATSI HGDRTQRERE KALEMFRSGR CPILVATAVA ARGLDIPNVT HVVNYDLPTD
     IDDYVHRIGR TGRAGNTGIA TAFFNRGNRG VVRDLLDLLK EANQEVPSFL ESIAREGSGF
     GGGGGRGGRG GGRGRGNAAT RDVRRMGGGG GAGGFGGGGW GGAPQGGYGG GYGGAPAGGY
     APPSGGAYGG GGGGGGGGGY GGGYGNPSGP GGNSWW
//
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