ID   IF4A2_MACFA             Reviewed;         408 AA.
AC   Q4R4Y9;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Eukaryotic initiation factor 4A-II;
DE            Short=eIF-4A-II;
DE            Short=eIF4A-II;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent RNA helicase eIF4A-2;
GN   Name=EIF4A2; ORFNames=QnpA-20305;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Parietal cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 EIF4G1/EIFFG3 (By similarity).
CC       Interacts with EIF4E. May interact with NOM1 (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; AB169755; BAE01836.1; -; mRNA.
DR   RefSeq; NP_001271641.1; NM_001284712.1.
DR   AlphaFoldDB; Q4R4Y9; -.
DR   SMR; Q4R4Y9; -.
DR   STRING; 9541.XP_005545521.1; -.
DR   GeneID; 101925544; -.
DR   CTD; 1974; -.
DR   eggNOG; KOG0327; Eukaryota.
DR   OrthoDB; 726081at2759; -.
DR   Proteomes; UP000233100; Unplaced.
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; cd18046; DEADc_EIF4AII_EIF4AI_DDX2; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR044728; EIF4A_DEADc.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
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; 2.
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   Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding.
FT   CHAIN           1..408
FT                   /note="Eukaryotic initiation factor 4A-II"
FT                   /id="PRO_0000054939"
FT   DOMAIN          65..236
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          247..408
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           34..62
FT                   /note="Q motif"
FT   MOTIF           183..186
FT                   /note="DEAD box"
FT   BINDING         77..84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         160
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14240"
SQ   SEQUENCE   408 AA;  46417 MW;  637003B8D9B15BE4 CRC64;
     MSGGSADYNS REHGGPEGMD PDGVIESNWN EIVDNFDDMN LKESLLRGIY AYGFEKPSAI
     QQRAIIPCIK GYDVIAQAQS GTGKTATFAI SILQQLEIEF KETQALVLAP TRELAQQIQK
     VILALGDYMG ATCHACIGGT NVRNEMQKLQ AEAPHIVVGT PGRVFDMLNR RYLSPKWIKM
     FVLDEADGML SRGFKDQIYE IFQKLNTSIQ VVLLSATMPT DVLEVTKKFM RDPIRILVKK
     EELTLEGIKQ FYINVEREEW KLDTLCDLYE TLTITQAVIF LNTRRKVDWL TEKMHARDFT
     VSALHGDMDQ KERDVIMREF RSGSSRVLIT TDLLARGIDV QQVSLVINYD LPTNRENYIH
     RIGRGGRFGR KGVAINFVTE EDKRILRDIE TFYNTTVEEM PMNVADLI