ID IF4A_PICST Reviewed; 397 AA.
AC A3GFI4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
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; ORFNames=PICST_74636;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; AAVQ01000001; EAZ63353.1; -; Genomic_DNA.
DR RefSeq; XP_001387376.1; XM_001387339.1.
DR AlphaFoldDB; A3GFI4; -.
DR SMR; A3GFI4; -.
DR STRING; 322104.A3GFI4; -.
DR GeneID; 4851033; -.
DR KEGG; pic:PICST_74636; -.
DR eggNOG; KOG0327; Eukaryota.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; A3GFI4; -.
DR OMA; FGCQALV; -.
DR OrthoDB; 1087080at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; 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: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; IEA:UniProtKB-KW.
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_0000285135"
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; 44720 MW; A6C77BBE47809EED CRC64;
MSSDGIKEID SDLIETNYDN VVYKFDDLNL KPNIVRGIFG YGYETPSAIQ QRAILPITEG
RDVLAQAQSG TGKTATFTIS ALQRIDENEK STQALILAPT RELALQIKNV ITSIGLYLNV
TVHASIGGTS MQDDIEAFRS GVQVVVGTPG RVFDMIERRY FKTEKVKMFI MDEADEMLSS
GFKEQIYNIF RLLPETTQVV LLSATMPQDV LEVTTKFMNN PVRILVKKDE LTLEGIKQFY
INVELEDYKF DCLCDLYDSI SVTQAVIFCN TRSKVEFLTT KLKAENFTVS AIHADLPQAE
RDTIMKEFRS GSSRILIATD LLARGIDVQQ VSLVINYDLP SNKENYIHRI GRGGRFGRKG
VAINFVTERD VGMMREIEQF YSTQIEEMPA DIGALFN
//
