ID E3RY72_PYRTT Unreviewed; 599 AA.
AC E3RY72;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=ATP-dependent RNA helicase DED1 {ECO:0000256|ARBA:ARBA00024397};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=ATP-dependent RNA helicase ded1 {ECO:0000256|ARBA:ARBA00024405};
DE Flags: Fragment;
GN ORFNames=PTT_14452 {ECO:0000313|EMBL:EFQ89342.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ89342.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ89342.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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.
CC {ECO:0000256|ARBA:ARBA00025161}.
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 Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC subfamily. {ECO:0000256|ARBA:ARBA00024358}.
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DR EMBL; GL535824; EFQ89342.1; -; Genomic_DNA.
DR RefSeq; XP_003302577.1; XM_003302529.1.
DR AlphaFoldDB; E3RY72; -.
DR STRING; 861557.E3RY72; -.
DR EnsemblFungi; EFQ89342; EFQ89342; PTT_14452.
DR KEGG; pte:PTT_14452; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_16_3_1; -.
DR OrthoDB; 5480645at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031370; F:eukaryotic initiation factor 4G binding; IEA:EnsemblFungi.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:EnsemblFungi.
DR GO; GO:0003724; F:RNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0033592; F:RNA strand annealing activity; IEA:EnsemblFungi.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IEA:EnsemblFungi.
DR GO; GO:1990625; P:negative regulation of cytoplasmic translational initiation in response to stress; IEA:EnsemblFungi.
DR GO; GO:1901195; P:positive regulation of formation of translation preinitiation complex; IEA:EnsemblFungi.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:EnsemblFungi.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IEA:EnsemblFungi.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF32; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022540};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT DOMAIN 196..224
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 227..418
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 429..590
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 196..224
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 9..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 599
FT /evidence="ECO:0000313|EMBL:EFQ89342.1"
SQ SEQUENCE 599 AA; 64269 MW; 5B1C56795D817CED CRC64;
MAEQLDMGRL NINDSQHNPQ NGFNGERSAY IPPHLRGRPQ GGPGGPGPAP MDGPPPMMNG
GGGLGGSAWG PAGHGPPPMN GAGGQAGGWA NAPNFTPRGR DGPQGGGGGW GGAPRGNFDP
NAYGKPGGGG SGGARGSGDG AWKDGKHVPG PPNQRLERDL FGVPNDPSKQ QTGINFEKYD
DIPVEASGQG VPEPVTRFTN PPLDDHLLSN IELSGYKVPT PVQKYSIPIV MGGRDLMACA
QTGSGKTGGF LFPILAQAFQ NGPSPPPQQA QGGYGRQRKA YPTSLVLAPT RELVSQIFDE
ARKFAYRSWV RPCVVYGGAD IGSQLRQIER GCDLLVATPG RLVDLIERGR ISLASIKYLV
LDEADRMLDM GFEPQIRRIV EGEDMPPTAG RQTLMFSATF PRDIQMLARD FLKDYIFLSV
GRVGSTSENI TQKIEYVEDV DKRSVLLDIL HTHDPTNLTL VFVETKRMAD SLSDFLINQG
FPATSIHGDR TQREREKALE MFRNGRCPIL VATAVAARGL DIPHVKHVVN YDLPTDIDDY
VHRIGRTGRA GNTGIATAFF NRGNRGVVRD LLELLKEANQ EVPGFLESIA REGSGFGGG
//
