DED1_PHANO
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 03-AUG-2022, entry version 86.
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) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC 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 and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- FUNCTION: ATP-binding RNA helicase involved in translation initiation.
CC Remodels RNA in response to ADP and ATP concentrations by facilitating
CC disruption, but also formation of RNA duplexes (By similarity).
CC {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 box
CC family of RNA helicases and controls ATP binding and 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};
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DR EMBL; CH445329; EAT89163.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001794501.1; XM_001794449.1.
DR AlphaFoldDB; Q0UWA6; -.
DR SMR; Q0UWA6; -.
DR STRING; 13684.SNOT_03958; -.
DR PRIDE; Q0UWA6; -.
DR GeneID; 5971364; -.
DR KEGG; pno:SNOG_03958; -.
DR eggNOG; KOG0335; Eukaryota.
DR InParanoid; Q0UWA6; -.
DR OMA; CYRSWVR; -.
DR OrthoDB; 595675at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
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; Reference proteome; RNA-binding.
FT CHAIN 1..696
FT /note="ATP-dependent RNA helicase DED1"
FT /id="PRO_0000255987"
FT DOMAIN 232..423
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 434..594
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 201..229
FT /note="Q motif"
FT MOTIF 367..370
FT /note="DEAD box"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 245..252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
