DHH1_PHANO
ID DHH1_PHANO Reviewed; 522 AA.
AC Q0U7S9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, 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=SNOG_12185;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT80597.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH445345; EAT80597.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001802414.1; XM_001802362.1.
DR AlphaFoldDB; Q0U7S9; -.
DR SMR; Q0U7S9; -.
DR STRING; 13684.SNOT_12185; -.
DR GeneID; 5979324; -.
DR KEGG; pno:SNOG_12185; -.
DR eggNOG; KOG0326; Eukaryota.
DR InParanoid; Q0U7S9; -.
DR OMA; TAIRIQI; -.
DR OrthoDB; 583315at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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:0003729; F:mRNA binding; IBA:GO_Central.
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:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
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..522
FT /note="ATP-dependent RNA helicase DHH1"
FT /id="PRO_0000255998"
FT DOMAIN 80..250
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 260..420
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 427..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 49..77
FT /note="Q motif"
FT MOTIF 198..201
FT /note="DEAD box"
FT COMPBIAS 429..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 522 AA; 58158 MW; B9A39558C18B5AD0 CRC64;
MTSEITNQMA STKLSDASAS TLADWKEGLK APAKDARPQT EDVTATKGLE FEDFFIKREL
MMGIFEAGFE KPSPIQEETI PVALTGRDIL ARAKNGTGKT AAFVIPTLER VNPKISKTQA
LILVPTRELA LQTSQVCKTL GKHLGINVMV STGGTGLKDD IIRLSDPVHI IVGTPGRILD
LAGKGVADLS TCQTFVMDEA DKLLSPEFTP VVEQLLGFHP KDRQVMLFSA TFPIVVKTFK
DKHMNSPYEI NLMDELTLRG ITQYYAFVEE KQKVHCLNTL FNKLQINQSI IFCNSTNRVE
LLAKKITELG YSCFYSHARM LQHNRNRVFH DFRNGVCRNL VCSDLLTRGI DIQAVNVVIN
FDFPKNAETY LHRIGRSGRF GHLGLAINLI NWEDRFNLYR IEQELGTEIQ PIPQVIEKNL
YVYESPENIP RPISSSQRQP GQQQEQDGTV VRNNQGQNPR GNFRGGRGGG GGGQFQGQRR
NPPPGQGQPQ QGQGMGQVQQ PRQNGQQAQR NPQRQPTGPP QA
