DHH1_YARLI
ID DHH1_YARLI Reviewed; 522 AA.
AC Q6C0X2; Q9UUU4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ATP-dependent RNA helicase DHH1;
DE EC=3.6.4.13;
GN Name=DHH1; OrderedLocusNames=YALI0F21032g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E 129;
RA Ferminan E., Dominguez A.;
RT "Isolation and characterization of YlDHH1 of Yarrowia lipolytica, a gene
RT encoding for a RNA helicase ATP dependent.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; AJ011564; CAB65518.1; -; Genomic_DNA.
DR EMBL; CR382132; CAG78499.1; -; Genomic_DNA.
DR RefSeq; XP_505690.1; XM_505690.1.
DR AlphaFoldDB; Q6C0X2; -.
DR SMR; Q6C0X2; -.
DR STRING; 4952.CAG78499; -.
DR EnsemblFungi; CAG78499; CAG78499; YALI0_F21032g.
DR GeneID; 2908268; -.
DR KEGG; yli:YALI0F21032g; -.
DR VEuPathDB; FungiDB:YALI0_F21032g; -.
DR HOGENOM; CLU_003041_30_0_1; -.
DR InParanoid; Q6C0X2; -.
DR OMA; TAIRIQI; -.
DR Proteomes; UP000001300; Chromosome F.
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_0000232193"
FT DOMAIN 59..229
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 239..399
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 28..56
FT /note="Q motif"
FT MOTIF 177..180
FT /note="DEAD box"
FT COMPBIAS 427..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..491
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 72..79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 163..164
FT /note="KG -> RK (in Ref. 1; CAB65518)"
FT /evidence="ECO:0000305"
FT CONFLICT 200..201
FT /note="ED -> WTT (in Ref. 1; CAB65518)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="L -> V (in Ref. 1; CAB65518)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="F -> S (in Ref. 1; CAB65518)"
FT /evidence="ECO:0000305"
FT CONFLICT 452..456
FT /note="VPPQG -> YLPRV (in Ref. 1; CAB65518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 58529 MW; 3447EC91408508F6 CRC64;
MSEWKESLNV PKKDTRHKTE DVTATKGTGF EDFFLKRELL MGIFEAGFEN PSPIQEEAIP
IALAGRDILA RAKNGTGKTA AFVIPALQQV NPKVNKIQAL IMVPTRELAL QTSQVCKTLG
KHLGIKVMVT TGGTNLRDDI MRLEDTVHVL VGTPGRVLDL AGKGVADLSE SPMFIMDEAD
KLLSPDFTPI IEQVLHFFPE DRQILLFSAT FPLTVKAFMD RNLHKPYEIN LMDELTLRGI
TQYYAFVDEK QKLHCLNTLF SKLDINQSII FCNSTVRVEL LARKITELGY SCYYSHAKMI
QSHRNRVFHE FRNGTCRNLV CSDLLTRGID IQAVNVVINF DFPKNAETYL HRIGRSGRFG
HLGIAINLIN WNDRYNLYKI EQELGTEIKP IPAQIDKNLY VAESSENIPR PFPIADMPRG
KESKRNEQFQ PQQNQNQQQQ QDGQNQHSLG PVPPQGPPQG IPGPGYGYPP PQGFPQGMPP
QGMPPQGAGG YMPPTPYGYQ QQGFPPQPPQ GFNNGQPQQP SQ
