ID   DHH1_CHAGB              Reviewed;         512 AA.
AC   Q2GQ93;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=ATP-dependent RNA helicase DHH1;
DE            EC=3.6.4.13;
GN   Name=DHH1; ORFNames=CHGG_09861;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408035; EAQ83457.1; -; Genomic_DNA.
DR   RefSeq; XP_001227788.1; XM_001227787.1.
DR   AlphaFoldDB; Q2GQ93; -.
DR   SMR; Q2GQ93; -.
DR   STRING; 38033.XP_001227788.1; -.
DR   EnsemblFungi; EAQ83457; EAQ83457; CHGG_09861.
DR   GeneID; 4396346; -.
DR   eggNOG; KOG0326; Eukaryota.
DR   HOGENOM; CLU_003041_30_2_1; -.
DR   InParanoid; Q2GQ93; -.
DR   OMA; VCADEAP; -.
DR   OrthoDB; 583315at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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..512
FT                   /note="ATP-dependent RNA helicase DHH1"
FT                   /id="PRO_0000255996"
FT   DOMAIN          42..212
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          222..382
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           11..39
FT                   /note="Q motif"
FT   MOTIF           160..163
FT                   /note="DEAD box"
FT   BINDING         55..62
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   512 AA;  57378 MW;  C3C87905A342CA02 CRC64;
     MDRDVTNTKG LDFEDFGLKR DLLMGIFEAG FEKPSPIQEE SIPVALVGRD ILARAKNGTG
     KTAAFVIPAL EKINPKVSKI QCLILVPTRE LAMQTSQVCK TLGKHLGINV MVTTGGTGLR
     DDIVRLQDPV HIVVGTPGRI LDLAGKQVAD LSECPMFIMD EADKLLSIEF TPVIEQLLRF
     HPKDRQVMLF SATFPISVKD FSDKNMTSPY EINLMDELTL RGITQYYAYV EEKQKVHCLN
     TLFSKLQINQ SIIFCNSTNR VELLAKKITE LGYSCFYSHA KMAQQARNRV FHDFRNGVCR
     NLVCSDLLTR GIDIQAVNVV INFDFPKNAE TYLHRIGRSG RYGHLGLAIN LINWDDRFNL
     YNIERDLGTE IQPIPQTIDK SLYVYENPES IPRPISNLKP AGIQQQQQLS IPSTAVGRLA
     GTGPPKRFWS VWPSRPRRVP RQSRPLWWPP WRTFPRLPAR AGWAPELRRP ARWPCAGPKP
     ADIPCSAGLG LSLSHLFGAL GGVLTIAISS PP