DHH1_CANGA
ID DHH1_CANGA Reviewed; 507 AA.
AC Q6FQU5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=ATP-dependent RNA helicase DHH1;
DE EC=3.6.4.13;
GN Name=DHH1; OrderedLocusNames=CAGL0I03476g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380955; CAG60336.1; -; Genomic_DNA.
DR RefSeq; XP_447399.1; XM_447399.1.
DR AlphaFoldDB; Q6FQU5; -.
DR SMR; Q6FQU5; -.
DR STRING; 5478.XP_447399.1; -.
DR EnsemblFungi; CAG60336; CAG60336; CAGL0I03476g.
DR GeneID; 2889178; -.
DR KEGG; cgr:CAGL0I03476g; -.
DR CGD; CAL0129533; CAGL0I03476g.
DR VEuPathDB; FungiDB:CAGL0I03476g; -.
DR eggNOG; KOG0326; Eukaryota.
DR HOGENOM; CLU_003041_30_2_1; -.
DR InParanoid; Q6FQU5; -.
DR OMA; VCADEAP; -.
DR Proteomes; UP000002428; Chromosome I.
DR GO; GO:0098562; C:cytoplasmic side of membrane; IEA:EnsemblFungi.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
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:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR GO; GO:0003729; F:mRNA binding; IEA:EnsemblFungi.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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:0033962; P:P-body assembly; IEA:EnsemblFungi.
DR GO; GO:0045727; P:positive regulation of translation; IEA:EnsemblFungi.
DR GO; GO:0010603; P:regulation of cytoplasmic mRNA processing body assembly; IEA:EnsemblFungi.
DR GO; GO:0034063; P:stress granule assembly; IEA:EnsemblFungi.
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..507
FT /note="ATP-dependent RNA helicase DHH1"
FT /id="PRO_0000232187"
FT DOMAIN 62..232
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 242..402
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 31..59
FT /note="Q motif"
FT MOTIF 180..183
FT /note="DEAD box"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 507 AA; 57695 MW; D1257FDD0172BFB1 CRC64;
MSEDNSWKTQ LNLPKKDTRP QTDDVLNTKG NSFEDFYLKR ELLMGIFEAG FEKPSPIQEE
AIPVAITGRD ILARAKNGTG KTAAFVIPTL EKIKPKLNKI QALIMVPTRE LALQTSQVIR
TLGRHCGVSC MVTTGGTNLR DDILRLNETV HVLVGTPGRV LDLASRKVAD LSECSLFVMD
EADKMLSRDF KTIIEQVLTF LPKAHQSLLF SATFPLTVKE FMVKHLHKPY EINLMEELTL
KGITQYYAFV EERQKLHCLN TLFSKLQINQ AIIFCNSTNR VELLAKKITD LGYSCYYSHA
RMKQQDRNKV FHDFRQGKVR TLVCSDLLTR GIDIQAVNVV INFDFPKTAE TYLHRIGRSG
RFGHLGLAIN LINWNDRFNL YKIEQELGTE IAAIPATIDK SLYVAEDDTA VPVPVPIEDP
HIVHQRRMQE QQQQQQQQQG QQGQQQGYPG QQAFIPPQQG QPQFMPVPQQ YMQMNQQQGM
PPNQQQPPAM GYPPQQLPTG YVAQQRY
