(data stored in ACNUC7421 zone)

SWISSPROT: DHH1_ASHGO

ID   DHH1_ASHGO              Reviewed;         484 AA.
AC   Q75BS4;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 105.
DE   RecName: Full=ATP-dependent RNA helicase DHH1;
DE            EC=3.6.4.13;
GN   Name=DHH1; OrderedLocusNames=ACR197W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA turnover, and
CC       more specifically in mRNA decapping by activating the decapping enzyme
CC       DCP1. Is involved in G1/S DNA-damage checkpoint recovery, probably
CC       through the regulation of the translational status of a subset of
CC       mRNAs. May also have a role in translation and mRNA nuclear export (By
CC       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}.
DR   EMBL; AE016816; AAS51423.1; -; Genomic_DNA.
DR   RefSeq; NP_983599.1; NM_208952.1.
DR   SMR; Q75BS4; -.
DR   STRING; 33169.AAS51423; -.
DR   PRIDE; Q75BS4; -.
DR   EnsemblFungi; AAS51423; AAS51423; AGOS_ACR197W.
DR   GeneID; 4619731; -.
DR   KEGG; ago:AGOS_ACR197W; -.
DR   HOGENOM; HOG000268797; -.
DR   InParanoid; Q75BS4; -.
DR   KO; K12614; -.
DR   OMA; DWNLMSS; -.
DR   Proteomes; UP000000591; Chromosome III.
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:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033962; P:cytoplasmic mRNA processing body assembly; IBA:GO_Central.
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:0010603; P:regulation of cytoplasmic mRNA processing body assembly; IEA:EnsemblFungi.
DR   GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
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;
DR   PRODOM; Q75BS4.
DR   SWISS-2DPAGE; Q75BS4.
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW   mRNA transport; Nucleotide-binding; Reference proteome; RNA-binding;
KW   Translation regulation; Transport.
FT   CHAIN           1..484
FT                   /note="ATP-dependent RNA helicase DHH1"
FT                   /id="PRO_0000227954"
FT   DOMAIN          60..230
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          240..400
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         73..80
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           29..57
FT                   /note="Q motif"
FT   MOTIF           178..181
FT                   /note="DEAD box"
FT   COMPBIAS        426..483
FT                   /note="Gln-rich"
SQ   SEQUENCE   484 AA;  54841 MW;  657CBCAD34D4311B CRC64;
     MSEDWKKKLN IPKKDTRPQT DDVLNTKGNT FEDFYLRREL LMGIFEAGFE RPSPIQEEAI
     PIALARRDIL ARAKNGTGKT AAFVIPTLEI VKPKVNKIQA LIMVPTRELA LQTSQVVRTL
     GKHCGISCMV TTGGTNLRDD IMRLNEPVHV LVGTPGRVLD LASRKVADLS ECSLFVMDEA
     DKMLSRDFKS LVEQILSFLP QNHQSLLFSA TFPLTVKEFM VKHLNKPYEI NLMDELTLKG
     ITQYYAFVEE RQKLHCLNTL FSKLQINQAI IFCNSTNRVE LLAKKITDLG YSCYYSHARM
     KQQERNKVFH EFRQGKVRTL VCSDLLTRGI DIQAVNVVIN FDFPKTAETY LHRIGRSGRF
     GHLGLAINLI NWNDRFNLYK IEQELGTEIA AIPAQIDKSL YVAEDTSAVP VPFPLDTMQG
     NARAAQQMPH PQQQAQLGGM PQPIPQQIQP PLAHQQAQPP PQVYPPQMYH QGIPPQQFAN
     PPQF
//

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