ID IF415_TOBAC Reviewed; 413 AA.
AC Q40468;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Eukaryotic initiation factor 4A-15;
DE Short=eIF-4A-15;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase eIF4A-15;
OS Nicotiana tabacum (Common 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=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. SR1;
RX PubMed=7858215; DOI=10.1007/bf00019489;
RA Owttrim G.W., Mandel T., Trachsel H., Thomas A.A., Kuhlemeier C.;
RT "Characterization of the tobacco eIF-4A gene family.";
RL Plant Mol. Biol. 26:1747-1757(1994).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X79138; CAA55739.1; -; mRNA.
DR PIR; S52020; S52020.
DR RefSeq; NP_001312859.1; NM_001325930.1.
DR AlphaFoldDB; Q40468; -.
DR SMR; Q40468; -.
DR STRING; 4097.Q40468; -.
DR PaxDb; 4097-Q40468; -.
DR GeneID; 107814763; -.
DR KEGG; nta:107814763; -.
DR OrthoDB; 1087080at2759; -.
DR Proteomes; UP000084051; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR CDD; cd17939; DEADc_EIF4A; 1.
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:SF146; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 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 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..413
FT /note="Eukaryotic initiation factor 4A-15"
FT /id="PRO_0000054961"
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; 46717 MW; 189A6EEF5D05E718 CRC64;
MAGAAPEGSQ FDARQFDTKM NELLSADGQD FFTSYDEVYD SFDAMGLQEN LLRGIYAYGF
EKPSAIQQRG IVPFCKGLDV IQQAQSGTGK TATFCSGILQ QLAYELLECQ ALVLAPTREL
AQQIEKVMRA LGDYLGVKVT ACVGGTSVRE DQRILSSGVH VVVGTPGRVF DMLRRQSLRP
DHIKMFVLDE ADEMLSRGFK DQIYDIFQLL PPKIQVGVFS ATMPPEALEI TRKFMNKPVR
ILVKRDELTL EGIKQFYVNV DKEEWKLETL CDLYETLAIT QSVIFVNTRR KVDWLTDKMR
SRDHTVSATH GDMDQNTRDI IMREFRSGSS RVLITTDLLA RGIDVQQVSL VINFDLPTQP
ENYLHRIGRS GRFGRKGVAI NFVTKDDERM LSDIQRFYNV VIEELPANVA DLL
//
