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Database: UniProt
Entry: Q8SQK9
LinkDB: Q8SQK9
Original site: Q8SQK9 
ID   DHH1_ENCCU              Reviewed;         487 AA.
AC   Q8SQK9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   28-JUN-2023, entry version 106.
DE   RecName: Full=ATP-dependent RNA helicase DHH1;
DE            EC=3.6.4.13;
GN   Name=DHH1; OrderedLocusNames=ECU09_1640;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GB-M1;
RX   PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA   Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA   Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT   "Identification of transcriptional signals in Encephalitozoon cuniculi
RT   widespread among Microsporidia phylum: support for accurate structural
RT   genome annotation.";
RL   BMC Genomics 10:607-607(2009).
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; AL590451; CAD27136.2; -; Genomic_DNA.
DR   RefSeq; XP_955717.1; XM_950624.1.
DR   AlphaFoldDB; Q8SQK9; -.
DR   SMR; Q8SQK9; -.
DR   STRING; 284813.Q8SQK9; -.
DR   VEuPathDB; MicrosporidiaDB:ECU09_1640; -.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; Q8SQK9; -.
DR   OrthoDB; 1087080at2759; -.
DR   Proteomes; UP000000819; Chromosome IX.
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   CDD; cd17940; DEADc_DDX6; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR47960:SF17; ATP-DEPENDENT RNA HELICASE DDX6-RELATED; 1.
DR   PANTHER; PTHR47960; DEAD-BOX ATP-DEPENDENT RNA HELICASE 50; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..487
FT                   /note="ATP-dependent RNA helicase DHH1"
FT                   /id="PRO_0000255995"
FT   DOMAIN          137..307
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          317..478
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           106..134
FT                   /note="Q motif"
FT   MOTIF           255..258
FT                   /note="DEAD box"
FT   COMPBIAS        1..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         150..157
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   487 AA;  53946 MW;  CDCB6C9E26342729 CRC64;
     MKSMIEGVKK DGKKGRRNDR KDSWDKDGFT QRGRAEKKPV DLAKIQGIQG QIGIGKNKGD
     GNRLDCGMDK EEAEDGKDIM RCRHLSPGGG GMKRLLSEDV RETEGIGWES LGLGPVLLKR
     IRDIGYDFPS PVQVASIPHV LGGKNLLVRS KNGTGKTASY IVPMLNMINS SELSIQGIIL
     VPIRELALQI SRNVKRMSEG TGVISAPVVG GTSMQDDIIR VSNGVHVMVG TPGRIVDLVE
     KRVGTLSKRV ILVFDEADKL LDVTFGETVT KLLDLLPREK QMLLYSATFP YFVTGFIRRY
     MKNPLCINLM KELAPVGVKQ FYTYVKPSEK LLCLKSLLLR LSINQCVIFC NSIKTVELLA
     MKITEMGLPS YFIHSKMAQE DRNIVFHNFL KGKCKILVAT DLITRGVDAP NTNYVINFDI
     SKSPESYLHR IGRAGRFGAP GVAISLVTTE EKEMLMDIEA KLGKEISPLS DKGLSRLHES
     NIDRNQG
//
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