ID   IF4A2_PONAB             Reviewed;         407 AA.
AC   Q5R4X1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
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;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR861119; CAH93195.1; -; mRNA.
DR   RefSeq; NP_001126879.1; NM_001133407.1.
DR   RefSeq; XP_009237907.1; XM_009239632.1.
DR   AlphaFoldDB; Q5R4X1; -.
DR   SMR; Q5R4X1; -.
DR   STRING; 9601.ENSPPYP00000016089; -.
DR   GeneID; 100173892; -.
DR   GeneID; 100189659; -.
DR   CTD; 1974; -.
DR   eggNOG; KOG0327; Eukaryota.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; Q5R4X1; -.
DR   OMA; EHKDGQR; -.
DR   TreeFam; TF101524; -.
DR   Proteomes; UP000001595; Chromosome 3.
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; 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   Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding.
FT   CHAIN           1..407
FT                   /note="Eukaryotic initiation factor 4A-II"
FT                   /id="PRO_0000054941"
FT   DOMAIN          64..235
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          246..407
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           33..61
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         159
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14240"
SQ   SEQUENCE   407 AA;  46402 MW;  FAA7D3BA9D8C6DA0 CRC64;
     MSGGSADYNR EHGGPEGMDP DGVIESNWNE IVDNFDDMNL KESLLRGIYA YGFEKPSAIQ
     QRAIIPCIKG YDVIAQAQSG TGKTATFAIS ILQQLEIEFK ETQALVLAPT RELAQQIQKV
     ILALGDYMGA TCHACIGGTN VRNEMQKLQA EAPHIVVGTP GRVFDMLNRR YLSPKWIKMF
     VLDEADEMLS RGFKDQIYEI FQKLNTSIQV VLLSATMPTD VLEVTKKFMR DPIRILVKKE
     ELTLEGIKQF YINVEREEWK LDTLCDLYET LTITQAVIFL NTRRKVDWLT EKMHARDFTV
     SALHGDMDQK ERDVIMREFR SGSSRVLITT DLLARGIDVQ QVSLVINYDL PTNRENYIHR
     IGRGGRFGRK GVAINFVTEE DKRILRDIET FYNTTVEEMP MNVADLI