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Database: UniProt
Entry: Q6FQQ6
LinkDB: Q6FQQ6
Original site: Q6FQQ6 
ID   IF4A_CANGA              Reviewed;         396 AA.
AC   Q6FQQ6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 101.
DE   RecName: Full=ATP-dependent RNA helicase eIF4A;
DE            EC=3.6.4.13;
DE   AltName: Full=Eukaryotic initiation factor 4A;
DE            Short=eIF-4A;
DE   AltName: Full=Translation initiation factor 1;
GN   Name=TIF1; Synonyms=TIF41; OrderedLocusNames=CAGL0I04356g;
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 which is a subunit of the eIF4F
CC       complex involved in cap recognition and is required for mRNA binding to
CC       ribosome. In the current model of translation initiation, eIF4A unwinds
CC       RNA secondary structures in the 5'-UTR of mRNAs which is necessary to
CC       allow efficient binding of the small ribosomal subunit, and subsequent
CC       scanning for the initiator codon (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   -!- SUBUNIT: Component of the eIF4F complex, which composition varies with
CC       external and internal environmental conditions. It is composed of at
CC       least eIF4A, eIF4E and eIF4G (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {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. eIF4A subfamily.
CC       {ECO:0000305}.
DR   EMBL; CR380955; CAG60375.1; -; Genomic_DNA.
DR   RefSeq; XP_447438.1; XM_447438.1.
DR   SMR; Q6FQQ6; -.
DR   STRING; 5478.XP_447438.1; -.
DR   PRIDE; Q6FQQ6; -.
DR   EnsemblFungi; CAG60375; CAG60375; CAGL0I04356g.
DR   GeneID; 2889047; -.
DR   KEGG; cgr:CAGL0I04356g; -.
DR   CGD; CAL0130157; TIF1.
DR   EuPathDB; FungiDB:CAGL0I04356g; -.
DR   eggNOG; KOG0327; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   InParanoid; Q6FQQ6; -.
DR   KO; K03257; -.
DR   OMA; RNPIRIL; -.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IDA:CGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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; 2.
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; Initiation factor;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT   CHAIN           1..396
FT                   /note="ATP-dependent RNA helicase eIF4A"
FT                   /id="PRO_0000232133"
FT   DOMAIN          54..223
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          234..395
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         67..74
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           23..51
FT                   /note="Q motif"
FT   MOTIF           171..174
FT                   /note="DEAD box"
SQ   SEQUENCE   396 AA;  44787 MW;  917BD19CF38B2167 CRC64;
     MSTDQMTQLD ESQIETNYDK VVYEFDDMNL NEKLLRGVFG YGFNKPSAIQ QRAIMPIIEG
     NDVLAQAQSG TGKTGTFSIA ALQRIDPAIK APQALMLAPT RELALQIQKV VMALGFHMDI
     KVHACIGGTS FVEDAEGLRD AQIVVGTPGR VFDNIQRRKF KVDNIKMFIL DEADEMLSTG
     FKEQIYQIFT MLPPTTQVVL LSATMPRDVL EVTAKFMQNP VRILVKKDEL TLEGIKQFYV
     NVEEEQFKYD CLTDLYDSIS VTQAVIFCNT RRKVEELTQR LTADNFTVSS IYSDLPQQER
     DTIMKEFRSG SSRILISTDL LARGIDVQQV SLVINYDLPT NKENYIHRIG RGGRFGRKGV
     AINFIVNEDV QALRELEQFY STQIEELPSD IGTLFT
//
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