ID   DHH1_NEUCR              Reviewed;         569 AA.
AC   Q7S5D9;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 3.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=ATP-dependent RNA helicase dhh1;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box RNA helicase 10;
GN   Name=drh-10; Synonyms=dhh1; ORFNames=NCU06149;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA turnover, and
CC       more specifically in mRNA decapping. Is involved in G1/S DNA-damage
CC       checkpoint recovery, probably through the regulation of the
CC       translational status of a subset of mRNAs. May also have a role in
CC       translation and mRNA nuclear export (By 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}.
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DR   EMBL; CM002242; EAA30775.3; -; Genomic_DNA.
DR   RefSeq; XP_960011.3; XM_954918.3.
DR   AlphaFoldDB; Q7S5D9; -.
DR   SMR; Q7S5D9; -.
DR   STRING; 367110.Q7S5D9; -.
DR   EnsemblFungi; EAA30775; EAA30775; NCU06149.
DR   GeneID; 3876149; -.
DR   KEGG; ncr:NCU06149; -.
DR   VEuPathDB; FungiDB:NCU06149; -.
DR   HOGENOM; CLU_003041_30_0_1; -.
DR   InParanoid; Q7S5D9; -.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR   GO; GO:0098562; C:cytoplasmic side of membrane; IEA:EnsemblFungi.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR   GO; GO:0000932; C:P-body; 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:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
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:0017148; P:negative regulation of translation; IBA:GO_Central.
DR   GO; GO:0045900; P:negative regulation of translational elongation; IEA:EnsemblFungi.
DR   GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
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; IBA:GO_Central.
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..569
FT                   /note="ATP-dependent RNA helicase dhh1"
FT                   /id="PRO_0000232192"
FT   DOMAIN          76..246
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          256..416
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           45..73
FT                   /note="Q motif"
FT   MOTIF           194..197
FT                   /note="DEAD box"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..569
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         89..96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   569 AA;  63735 MW;  9D441F9133E7FCBC CRC64;
     MSDQLADQLK ATSLSSGPED WKKGLNLPAR DTRQQTEDVT NTRGLDWEDF IHDRDLLMGI
     FEAGFEKPSP IQEEAIPVAL TGRDILARAK NGTGKTAAFV IPALNKINPK VSKIQCLILV
     PTRELAMQTS QVCKTLGKHL GINVMVTTGG TGLRDDIVRL QDPVHIVVGT PGRILDLAGK
     QVADLSECPM FIMDEADKLL SQEFTPVIEQ LLQFHPKDRQ VMLFSATFPL SVKDFSDKNM
     TSPYEINLMD ELTLRGITQY YAFVEEKQKV HCLNTLFSKL QINQSIIFCN STNRVELLAK
     KITELGYSCF YSHAKMAQQA RNRVFHDFRN GVCRNLVCSD LLTRGIDIQA VNVVINFDFP
     KNAETYLHRI GRSGRYGHLG LAINLINWDD RFNLYNIERD LGTEIQPIPQ TIDKSLYVYE
     NPESIPRPIS TFKPIAQQPQ QQLQQSQRPQ QSQQQQHFST QTQPSNQLPP QQGNQQLGFN
     PQAQQPHRPI PQAQGDWQGQ NGRQNGTGAS NNQPRPTNYQ NNRGQPGSSR GGRGRGFQGQ
     GGRQNQNYGG QRGPRTQGQG QPQGPLSAQ