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IF4A1_BOVIN
ID   IF4A1_BOVIN             Reviewed;         406 AA.
AC   Q3SZ54;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Eukaryotic initiation factor 4A-I;
DE            Short=eIF-4A-I;
DE            Short=eIF4A-I;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent RNA helicase eIF4A-1;
GN   Name=EIF4A1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-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/EIF4G3. Interacts with
CC       PAIP1, EIF4E and UPF2. Found in a complex with XPO7, EIF4A1, ARHGAP1,
CC       VPS26A, VPS29, VPS35 and SFN. May interact with NOM1. Interacts with
CC       PDCD4; this interferes with the interaction between EIF4A and EIF4G.
CC       Interacts with RBM4 (By similarity). Interacts with DDX3X in an RNA-
CC       independent manner (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P60842}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC103130; AAI03131.1; -; mRNA.
DR   RefSeq; NP_001029400.1; NM_001034228.1.
DR   AlphaFoldDB; Q3SZ54; -.
DR   SMR; Q3SZ54; -.
DR   STRING; 9913.ENSBTAP00000000144; -.
DR   PaxDb; Q3SZ54; -.
DR   PeptideAtlas; Q3SZ54; -.
DR   PRIDE; Q3SZ54; -.
DR   Ensembl; ENSBTAT00000000144; ENSBTAP00000000144; ENSBTAG00000000132.
DR   GeneID; 504958; -.
DR   KEGG; bta:504958; -.
DR   CTD; 1973; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000132; -.
DR   VGNC; VGNC:28404; EIF4A1.
DR   eggNOG; KOG0327; Eukaryota.
DR   GeneTree; ENSGT00940000153889; -.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; Q3SZ54; -.
DR   OMA; HLGDYMN; -.
DR   OrthoDB; 726081at2759; -.
DR   TreeFam; TF101524; -.
DR   Reactome; R-BTA-1169408; ISG15 antiviral mechanism.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000000132; Expressed in spermatocyte and 107 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
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; 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   Acetylation; ATP-binding; Helicase; Hydrolase; Initiation factor;
KW   Isopeptide bond; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; RNA-binding; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   CHAIN           2..406
FT                   /note="Eukaryotic initiation factor 4A-I"
FT                   /id="PRO_0000244559"
FT   DOMAIN          63..234
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          245..406
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           32..60
FT                   /note="Q motif"
FT   MOTIF           182..185
FT                   /note="DEAD box"
FT   BINDING         76..83
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   MOD_RES         118
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   MOD_RES         158
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   MOD_RES         174
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   MOD_RES         193
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P60843"
FT   MOD_RES         238
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P60843"
FT   CROSSLNK        146
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   CROSSLNK        225
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   CROSSLNK        238
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   CROSSLNK        309
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   CROSSLNK        369
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
FT   CROSSLNK        381
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P60842"
SQ   SEQUENCE   406 AA;  46154 MW;  6EF89939F3045420 CRC64;
     MSASQDSRSR DNGPDGMEPE GVIESNWNEI VDSFDDMNLS ESLLRGIYAY GFEKPSAIQQ
     RAILPCIKGY DVIAQAQSGT GKTATFAISI LQQIELDLKA TQALVLAPTR ELAQQIQKVV
     MALGDYMGAS CHACIGGTNV RAEVQKLQME APHIIVGTPG RVFDMLNRRY LSPKYIKMFV
     LDEADEMLSR GFKDQIYDIF QKLNSNTQVV LLSATMPSDV LEVTKKFMRD PIRILVKKEE
     LTLEGIRQFY INVEREEWKL DTLCDLYETL TITQAVIFIN TRRKVDWLTE KMHARDFTVS
     AMHGDMDQKE RDVIMREFRS GSSRVLITTD LLARGIDVQQ VSLVINYDLP TNRENYIHRI
     GRGGRFGRKG VAINMVTEED KRTLRDIETF YNTSIEEMPL NVADLI
 
 
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