ID   DHH1_MAGO7              Reviewed;         535 AA.
AC   A4R715; G4N8U3;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=ATP-dependent RNA helicase DHH1;
DE            EC=3.6.4.13;
GN   Name=DHH1; ORFNames=MGG_03388;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA turnover, and
CC       more specifically in mRNA decapping by activating the decapping enzyme
CC       DCP1. Is involved in G1/S DNA-damage checkpoint recovery, probably
CC       through the regulation of the translational status of a subset of
CC       mRNAs. May also have a role in translation and mRNA nuclear export (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, P-body {ECO:0000250}. Note=Is
CC       concentrated in several cytoplasmic foci called P bodies (or
CC       cytoplasmic processing bodies) which represent sites of mRNA decapping
CC       and 5' to 3' exonucleotidic decay. {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. DDX6/DHH1
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001234; EHA50237.1; -; Genomic_DNA.
DR   RefSeq; XP_003716556.1; XM_003716508.1.
DR   AlphaFoldDB; A4R715; -.
DR   SMR; A4R715; -.
DR   STRING; 318829.MGG_03388T0; -.
DR   PRIDE; A4R715; -.
DR   EnsemblFungi; MGG_03388T0; MGG_03388T0; MGG_03388.
DR   GeneID; 2676879; -.
DR   KEGG; mgr:MGG_03388; -.
DR   VEuPathDB; FungiDB:MGG_03388; -.
DR   eggNOG; KOG0326; Eukaryota.
DR   HOGENOM; CLU_003041_30_0_1; -.
DR   InParanoid; A4R715; -.
DR   OMA; VCADEAP; -.
DR   OrthoDB; 583315at2759; -.
DR   Proteomes; UP000009058; Chromosome 4.
DR   GO; GO:0098562; C:cytoplasmic side of membrane; IEA:EnsemblFungi.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0003729; F:mRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:EnsemblFungi.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0045900; P:negative regulation of translational elongation; IEA:EnsemblFungi.
DR   GO; GO:0033962; P:P-body assembly; IEA:EnsemblFungi.
DR   GO; GO:0045727; P:positive regulation of translation; IEA:EnsemblFungi.
DR   GO; GO:0010603; P:regulation of cytoplasmic mRNA processing body assembly; IEA:EnsemblFungi.
DR   GO; GO:0034063; P:stress granule assembly; IEA:EnsemblFungi.
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; mRNA processing;
KW   mRNA transport; Nucleotide-binding; Reference proteome; RNA-binding;
KW   Translation regulation; Transport.
FT   CHAIN           1..535
FT                   /note="ATP-dependent RNA helicase DHH1"
FT                   /id="PRO_0000294620"
FT   DOMAIN          78..248
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          258..418
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          429..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           47..75
FT                   /note="Q motif"
FT   MOTIF           196..199
FT                   /note="DEAD box"
FT   COMPBIAS        432..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..535
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         91..98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   535 AA;  59996 MW;  8820E4EEA80B3666 CRC64;
     MADVLADQLR SATLSDATNN EDWRRNLNIP ARDNRQQTED VTNTKGLEFE NFGLKRDLLM
     GIFEAGFEKP SPIQEESIPV ALTGRDILAR AKNGTGKTAA FVVPALETIN PKVSKIQCLI
     LVPTRELAMQ TSQVCKTLGK HLGINVMVTT GGTTLRDDIL RLQDPVHIVV GTPGRILDLA
     GKNVADLSEC PMFIMDEADK LLSIEFTPVI EQLLQFHPKD RQVMLFSATF PISVKEFSDK
     NMTNPYEINL MDELTLRGIT QYYAFVEEKQ KVHCLNTLFS KLQINQSIIF CNSTNRVELL
     AKKITELGYS CFYSHAKMQQ QARNRVFHDF RNGVCRNLVC SDLLTRGIDI QAVNVVINFD
     FPKNAETYLH RIGRSGRYGH LGLAINLISW EDRFNLYNIE RDLGTEIQPI PSTIDKSLYV
     YDNPETIPRP INIPAQPSSA GNAQSAAPNQ GPPPQQQRPH QGQENWQNQN GRHNGSSQQQ
     QPRGPHQNRG RGGGRGRGGF QGQGQGQRNY NNNYRGGRGG HNQGQHQQQM PNQQS