IF4A_WHEAT
ID IF4A_WHEAT Reviewed; 414 AA.
AC P41378;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Eukaryotic initiation factor 4A;
DE Short=eIF-4A;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase eIF4A;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8406026; DOI=10.1016/0378-1119(93)90310-y;
RA Metz A.M., Browning K.S.;
RT "Sequence of a cDNA encoding wheat eukaryotic protein synthesis initiation
RT factor 4A.";
RL Gene 131:299-300(1993).
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.
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; Z21510; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; JN0839; JN0839.
DR AlphaFoldDB; P41378; -.
DR SMR; P41378; -.
DR STRING; 4565.Traes_7DL_6AC3E4622.2; -.
DR ChEMBL; CHEMBL3308965; -.
DR PRIDE; P41378; -.
DR eggNOG; KOG0327; Eukaryota.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P41378; baseline and differential.
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 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; Reference proteome; RNA-binding.
FT CHAIN 1..414
FT /note="Eukaryotic initiation factor 4A"
FT /id="PRO_0000054964"
FT DOMAIN 72..242
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 253..414
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 41..69
FT /note="Q motif"
FT MOTIF 190..193
FT /note="DEAD box"
FT BINDING 85..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 414 AA; 46928 MW; 88CFEC8BF56C867F CRC64;
MAGMAPEGSQ FDAKNYDSKM QELLSQGETE EFFTSYDEVH ESFDDMGLQE NLLRGIYAYG
FEKPSAIQQR GIVPFCKGLD VIQQAQSGTG KTATFCSGIL QQLDYGLVEC QALVLAPTRE
LAQQIEKVMR ALGDYLGVKV HACVGGTSVR EDQRILASGV HVVVGTPGRV FDIVRRQSLR
PDNIKMFVLD EADEMLSRGF KDQIYDIFQL LPGKIQVGVF SATMPPEALE ITRKFMNKPV
RILVKRDELT LEGIKQFYVN VEKEEWKLDT LCDLYETLAI TQSVIFVNTR RKVDWLTDKM
RGRDHTVSAT HGDMDQNTRD IIMREFRSGS SRVLITTDLL ARGIDVQQVS LVINYDLPTQ
PENYQHRIGR SGRFGRKGVA INFVTREDER MLFDIQKFYN VVIEELPANV ADLL