DHH1_ENCCU
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 03-AUG-2022, entry version 103.
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 GeneID; 860503; -.
DR KEGG; ecu:ECU09_1640; -.
DR VEuPathDB; MicrosporidiaDB:ECU09_1640; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q8SQK9; -.
DR OrthoDB; 583315at2759; -.
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 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..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
