ID   IF4A2_NICPL             Reviewed;         413 AA.
AC   P41379;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Eukaryotic initiation factor 4A-2;
DE            Short=eIF-4A-2;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent RNA helicase eIF4A-2;
OS   Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root;
RX   PubMed=1719476; DOI=10.1093/nar/19.20.5491;
RA   Owttrim G.W., Hofmann S., Kuhlemeier C.;
RT   "Divergent genes for translation initiation factor eIF-4A are coordinately
RT   expressed in tobacco.";
RL   Nucleic Acids Res. 19:5491-5496(1991).
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: eIF4F is a multi-subunit complex, the composition of which
CC       varies with external and internal environmental conditions. It is
CC       composed of at least EIF4A, EIF4E and EIF4G (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X61205; CAA43513.1; -; mRNA.
DR   PIR; S22578; S22578.
DR   AlphaFoldDB; P41379; -.
DR   SMR; P41379; -.
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   Gene3D; 3.40.50.300; -; 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   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   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Hydrolase; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; RNA-binding.
FT   CHAIN           1..413
FT                   /note="Eukaryotic initiation factor 4A-2"
FT                   /id="PRO_0000054951"
FT   DOMAIN          71..241
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          252..413
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           40..68
FT                   /note="Q motif"
FT   MOTIF           189..192
FT                   /note="DEAD box"
FT   BINDING         84..91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   413 AA;  46829 MW;  14FFB327967BB2D4 CRC64;
     MAGSAPEGSQ FDARQFDAKM TELLGTEQEE FFTSYDEVYD SFDAMGLQEN LLRGIYAYGF
     EKPSAIQQRG IVPFCKGLDV IQQAQSGTGK TATFCSGVLQ QLDYSLVECQ ALVLAPTREL
     AQQIEKVMRA LGDYLGVKVH ACVGGTSVRE DQRILQSGVH VVVGTPGRVF DMLRRQSLRP
     DHIKMFVLDE ADEMLSRGFK DQIYDIFQLL PPKIQVGVFS ATMPPEALEI TRKFMNKPVR
     ILVKRDELTL EGIKQFYVNV DKEEWKLETL CDLYETLAIT QSVIFVNTRR KVDWLTDKMR
     SRDHTVSATH GDMDQNTRDI IMREFRSGSS RVLITTDLLA RGIDVQQVSL VINYDLPTQP
     ENYLHRIGRS GRFGRKGVAI NSVTKDDERM LFDIQKFYNV VIEELPANVA DLL