ID DHH1_CANAL Reviewed; 549 AA.
AC Q5AAW3; A0A1D8PE02;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=ATP-dependent RNA helicase DHH1;
DE EC=3.6.4.13;
GN Name=DHH1; OrderedLocusNames=CAALFM_C107070CA;
GN ORFNames=CaO19.13577, CaO19.6197;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017623; AOW26359.1; -; Genomic_DNA.
DR RefSeq; XP_718788.1; XM_713695.1.
DR AlphaFoldDB; Q5AAW3; -.
DR SMR; Q5AAW3; -.
DR BioGRID; 1222584; 1.
DR STRING; 237561.Q5AAW3; -.
DR EnsemblFungi; C1_07070C_A-T; C1_07070C_A-T-p1; C1_07070C_A.
DR GeneID; 3639490; -.
DR KEGG; cal:CAALFM_C107070CA; -.
DR CGD; CAL0000182112; DHH1.
DR VEuPathDB; FungiDB:C1_07070C_A; -.
DR eggNOG; KOG0326; Eukaryota.
DR HOGENOM; CLU_003041_30_2_1; -.
DR InParanoid; Q5AAW3; -.
DR OMA; ECPLFVM; -.
DR OrthoDB; 1087080at2759; -.
DR PRO; PR:Q5AAW3; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0098562; C:cytoplasmic side of membrane; IEA:EnsemblFungi.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:CGD.
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:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
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:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0045900; P:negative regulation of translational elongation; IEA:EnsemblFungi.
DR GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
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; IBA:GO_Central.
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..549
FT /note="ATP-dependent RNA helicase DHH1"
FT /id="PRO_0000232186"
FT DOMAIN 61..231
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 241..401
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 30..58
FT /note="Q motif"
FT MOTIF 179..182
FT /note="DEAD box"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..527
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 549 AA; 62110 MW; 1AA169EF435AA0BF CRC64;
MTDTNWKQNL NLPPKDTRPQ TEDVLNTKGK SFEDFNLKRE LLMGIFEAGF EKPSPIQEES
IPMALAGRDI LARAKNGTGK TASFIIPCLQ LVKPKLNKVQ ALILVPTREL ALQTSQVVRT
LGKHVGTQCM VTTGGTSLRD DIVRLHDPVH ILVGTPGRVL DLAARKVVDL SECPLFVMDE
ADKMLSREFK GIIEQILEFF PPNRQALLFS ATFPLAVKSF MDKHLTKPYE INLMDELTLK
GISQFYAFVE EKQKLHCLNT LFSKLQINQS IIFCNSTNRV ELLAKKITEL GYSCYYSHAK
MPQQARNKVF HEFRQGKVRN LVCSDLLTRG IDIQAVNVVI NFDFPKTAET YLHRIGRSGR
FGHLGLAINL MSWNDRYSLY KIEQELGTEI KPIPATIDKS LYVAENADAV PRPFRIDELP
KGNETVHNKG YQYKGQPVKD ENSGSSSQQQ QQPPPQQQQQ QSTSPPQQQP QQQQQQPNPQ
HQFAPHPNGQ FPPYPQQFHQ PGAIPPQQFN GYPPYPQYPP QFAGYPGQPP QLPQGQQQHA
QAQNPAQQY
//
