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Database: UniProt
Entry: IF4A_CANAL
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Original site: IF4A_CANAL 
ID   IF4A_CANAL              Reviewed;         397 AA.
AC   P87206; A0A1D8PCG1; Q5A910;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 132.
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=TIF, TIF41; OrderedLocusNames=CAALFM_C101350CA;
GN   ORFNames=CaO19.10834, CaO19.3324;
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 [GENOMIC DNA].
RX   PubMed=8971628; DOI=10.1080/02681219680000701;
RA   Mirbod F., Nakashima S., Kitajima Y., Ghannoum M.A., Cannon R.D.,
RA   Nozawa Y.;
RT   "Molecular cloning of a gene encoding translation initiation factor (TIF)
RT   from Candida albicans.";
RL   J. Med. Vet. Mycol. 34:393-400(1996).
RN   [2]
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   [3]
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   [4]
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 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}.
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DR   EMBL; D84472; BAA20371.1; -; Genomic_DNA.
DR   EMBL; CP017623; AOW25828.1; -; Genomic_DNA.
DR   RefSeq; XP_718147.1; XM_713054.1.
DR   AlphaFoldDB; P87206; -.
DR   SMR; P87206; -.
DR   BioGRID; 1223011; 10.
DR   STRING; 237561.P87206; -.
DR   EnsemblFungi; C1_01350C_A-T; C1_01350C_A-T-p1; C1_01350C_A.
DR   GeneID; 3640190; -.
DR   KEGG; cal:CAALFM_C101350CA; -.
DR   CGD; CAL0000186279; TIF.
DR   VEuPathDB; FungiDB:C1_01350C_A; -.
DR   eggNOG; KOG0327; Eukaryota.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; P87206; -.
DR   OMA; FGCQALV; -.
DR   OrthoDB; 1087080at2759; -.
DR   PRO; PR:P87206; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0010494; C:cytoplasmic stress granule; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:CGD.
DR   GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR   GO; GO:0006413; P:translational initiation; ISS:CGD.
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; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF1; EUKARYOTIC TRANSLATION INITIATION FACTOR EIF-4A; 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; Initiation factor;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT   CHAIN           1..397
FT                   /note="ATP-dependent RNA helicase eIF4A"
FT                   /id="PRO_0000054965"
FT   DOMAIN          54..224
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          235..396
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           23..51
FT                   /note="Q motif"
FT   MOTIF           172..175
FT                   /note="DEAD box"
FT   BINDING         67..74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   397 AA;  44599 MW;  A81935EA752DDD60 CRC64;
     MASEGITEID SGLIETNYDN VVYKFDDLNL KPNIVRGIFG YGYETPSAIQ QRAILPITEG
     RDVLAQAQSG TGKTATFTIS ALQRINENEK ATQALILAPT RELALQIKNV ITAIGLYLKV
     TVHASIGGTS MSDDIEAFRS GVQIVVGTPG RVLDMIERRY FKTDKVKMFI LDEADEMLSS
     GFKEQIYNIF RLLPETTQIV LLSATMPQDV LEVTTKFMNN PVRILVKKDE LTLEGIKQFY
     INVELEDYKF DCLCDLYDSI SVTQAVIFCN TRSKVEFLTN KLREQHFTVS AIHADLPQAE
     RDTIMKEFRS GSSRILISTD LLARGIDVQQ VSLVINYDLP ANKENYIHRI GRGGRFGRKG
     VAINFVTDRD VGMMREIEKF YSTQIEEMPA DIGALFA
//
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