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Database: UniProt
Entry: Q5AAW3
LinkDB: Q5AAW3
Original site: Q5AAW3 
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   16-OCT-2019, entry version 88.
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;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   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.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., 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
RT   aligned on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
RP   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
RT   allele-specific measurements and provides a simple model for repeat
RT   and indel structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA turnover,
CC       and more specifically in mRNA decapping. Is involved in G1/S DNA-
CC       damage 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).
CC       {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
CC       decapping and 5' to 3' exonucleotidic decay. {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1
CC       subfamily. {ECO:0000305}.
DR   EMBL; CP017623; AOW26359.1; -; Genomic_DNA.
DR   RefSeq; XP_718788.1; XM_713695.1.
DR   SMR; Q5AAW3; -.
DR   BioGrid; 1222584; 1.
DR   STRING; 5476.C4YDW1; -.
DR   PRIDE; Q5AAW3; -.
DR   GeneID; 3639490; -.
DR   KEGG; cal:CAALFM_C107070CA; -.
DR   CGD; CAL0000182112; DHH1.
DR   EuPathDB; FungiDB:C1_07070C_A; -.
DR   InParanoid; Q5AAW3; -.
DR   KO; K12614; -.
DR   OMA; DWNLMSS; -.
DR   OrthoDB; 583315at2759; -.
DR   PRO; PR:Q5AAW3; -.
DR   Proteomes; UP000000559; Chromosome 1.
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:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033962; P:cytoplasmic mRNA processing body assembly; IBA:GO_Central.
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   GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
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; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   mRNA processing; mRNA transport; Nucleotide-binding;
KW   Reference proteome; RNA-binding; Translation regulation; Transport.
FT   CHAIN         1    549       ATP-dependent RNA helicase DHH1.
FT                                /FTId=PRO_0000232186.
FT   DOMAIN       61    231       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      241    401       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      74     81       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        30     58       Q motif.
FT   MOTIF       179    182       DEAD box.
FT   COMPBIAS    448    548       Gln-rich.
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
//
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