ID   DHH1_ASPTN              Reviewed;         509 AA.
AC   Q0CBE1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=ATP-dependent RNA helicase dhh1;
DE            EC=3.6.4.13;
GN   Name=dhh1; ORFNames=ATEG_08993;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476606; EAU31125.1; -; Genomic_DNA.
DR   RefSeq; XP_001217579.1; XM_001217578.1.
DR   AlphaFoldDB; Q0CBE1; -.
DR   SMR; Q0CBE1; -.
DR   STRING; 341663.Q0CBE1; -.
DR   EnsemblFungi; EAU31125; EAU31125; ATEG_08993.
DR   GeneID; 4323383; -.
DR   VEuPathDB; FungiDB:ATEG_08993; -.
DR   eggNOG; KOG0326; Eukaryota.
DR   HOGENOM; CLU_003041_30_0_1; -.
DR   OMA; VCADEAP; -.
DR   OrthoDB; 583315at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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..509
FT                   /note="ATP-dependent RNA helicase dhh1"
FT                   /id="PRO_0000282463"
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          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..509
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        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..509
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   509 AA;  57103 MW;  96DB1E59899EDA80 CRC64;
     MADALASQLN NTSLGDANSD AKWKDQLKTP AKDARPQTED VTATKGLEFE DFYIKRELMM
     GIFEAGFEKP SPIQEETIPV ALTGRDILAR AKNGTGKTAA FVIPTLERIN PKSTKTQALI
     LVPTRELALQ TSHVCKTLGK HLGINVMVTT GGTGLMDDII RLNDAVHILV GTPGRVLDLA
     SKGVADLSEC PTFVMDEADK LLSPEFTPVI EQLLSFHPKD RQVMLFSATF PLIVKSFKDK
     HMRNPYEINL MDELTLRGIT QYYAFVEEKQ KVHCLNTLFS KLQINQSIIF CNSTNRVELL
     AKKITELGYS CFYSHARMLQ QHRNRVFHDF RNGVCRNLVC SDLLTRGIDI QAVNVVINFD
     FPKNAETYLH RIGRSGRFGH LGLAINLINW DDRFNLYKIE QELGTEIQPI PQNIDKKLYV
     YDSPDTIPRP ISNPSQPPQA TGMPSGQHIG DRRHNNHPNG GHYQYNRGRG SYRGGRGQGP
     RRNVQHDQNR YNASQGQHQS GKSQAAPVS