ID   DHH1_NEOFI              Reviewed;         507 AA.
AC   A1D8G1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=ATP-dependent RNA helicase dhh1;
DE            EC=3.6.4.13;
GN   Name=dhh1; ORFNames=NFIA_071760;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027690; EAW22005.1; -; Genomic_DNA.
DR   RefSeq; XP_001263902.1; XM_001263901.1.
DR   AlphaFoldDB; A1D8G1; -.
DR   SMR; A1D8G1; -.
DR   STRING; 36630.CADNFIAP00005976; -.
DR   EnsemblFungi; EAW22005; EAW22005; NFIA_071760.
DR   GeneID; 4590548; -.
DR   KEGG; nfi:NFIA_071760; -.
DR   VEuPathDB; FungiDB:NFIA_071760; -.
DR   eggNOG; KOG0326; Eukaryota.
DR   HOGENOM; CLU_003041_30_0_1; -.
DR   OMA; VCADEAP; -.
DR   OrthoDB; 583315at2759; -.
DR   Proteomes; UP000006702; 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..507
FT                   /note="ATP-dependent RNA helicase dhh1"
FT                   /id="PRO_0000282464"
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..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..507
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        428..449
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..507
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   507 AA;  57178 MW;  10594CCBD1A6EFF2 CRC64;
     MADALANQLN NTSLGEANSE MRWREQLNMP AKDARPQTED VTATKGLEFE DFYIKRELMM
     GIFEAGFEKP SPIQEETIPV ALTGRDILAR AKNGTGKTAA FVIPTLERIN PKSTKTQALI
     LVPTRELALQ TSQVCKTLGK 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
     YDSPETIPRP ISNPSQPRQI TNTPANTSTA DRRHHNHPNN GQYQFNRGRG SYRGRGQGQR
     RSAQTETNKF GHPQGQHSGK TSTAPVS