GenomeNet

Database: UniProt
Entry: P29562
LinkDB: P29562
Original site: P29562 
ID   IF4A1_RABIT             Reviewed;         398 AA.
AC   P29562;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 2.
DT   18-SEP-2019, entry version 117.
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;
DE   Flags: Fragment;
GN   Name=EIF4A1; Synonyms=DDX2A, EIF4A;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 5-398, AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2241157; DOI=10.1016/0003-9861(90)90130-q;
RA   Conroy S.C., Dever T.E., Owens C.L., Merrick W.C.;
RT   "Characterization of the 46,000-dalton subunit of eIF-4F.";
RL   Arch. Biochem. Biophys. 282:363-371(1990).
CC   -!- FUNCTION: ATP-dependent RNA helicase which is a subunit of the
CC       eIF4F complex involved in cap recognition and is required for mRNA
CC       binding to ribosome. In the current model of translation
CC       initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR
CC       of mRNAs which is necessary to allow efficient binding of the
CC       small ribosomal subunit, and subsequent scanning for the initiator
CC       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
CC       which varies with external and internal environmental conditions.
CC       It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3.
CC       Interacts with PAIP1, EIF4E and UPF2. Found in a complex with
CC       XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. May interact
CC       with NOM1. Interacts with PDCD4; this interferes with the
CC       interaction between EIF4A and EIF4G. Interacts with RBM4 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A
CC       subfamily. {ECO:0000305}.
DR   PIR; S13269; S13269.
DR   SMR; P29562; -.
DR   STRING; 9986.ENSOCUP00000008940; -.
DR   ChEMBL; CHEMBL2052029; -.
DR   PRIDE; P29562; -.
DR   eggNOG; KOG0327; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000268797; -.
DR   InParanoid; P29562; -.
DR   BRENDA; 3.6.4.13; 1749.
DR   SABIO-RK; P29562; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005524; F:ATP 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   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   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Complete proteome;
KW   Direct protein sequencing; Helicase; Hydrolase; Initiation factor;
KW   Isopeptide bond; Nucleotide-binding; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome; RNA-binding;
KW   Ubl conjugation.
FT   CHAIN        <1    398       Eukaryotic initiation factor 4A-I.
FT                                /FTId=PRO_0000054937.
FT   DOMAIN       55    226       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      237    398       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      68     75       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        24     52       Q motif.
FT   MOTIF       174    177       DEAD box.
FT   MOD_RES     110    110       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P60842}.
FT   MOD_RES     150    150       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P60842}.
FT   MOD_RES     166    166       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P60842}.
FT   MOD_RES     185    185       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P60843}.
FT   MOD_RES     230    230       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P60843}.
FT   CROSSLNK    138    138       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P60842}.
FT   CROSSLNK    217    217       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P60842}.
FT   CROSSLNK    230    230       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P60842}.
FT   CROSSLNK    301    301       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P60842}.
FT   CROSSLNK    361    361       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P60842}.
FT   CROSSLNK    373    373       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P60842}.
FT   NON_TER       1      1
SQ   SEQUENCE   398 AA;  45291 MW;  8CE1C18DE7AC7D37 CRC64;
     SRDNGPDGME PEGVIESNWN EIVDSFDDMN LSESLLRGIY AYGFEKPSAI QQRAILPCIK
     GYDVIAQAQS GTGKTATFAI SILQQIELDL KATQALVLAP TRELAQQIQK VVMALGDYMG
     ASCHACIGGT NVRAEVQKLQ MEAPHIIVGT PGRVFDMLNR RYLSPKYIKM FVLDEADEML
     SRGFKDQIYD IFQKLNSNTQ VVLLSATMPS DVLEVTKKFM RDPIRILVKK EELTLEGIRQ
     FYINVEREEW KLDTLCDLYE TLTITQAVIF INTRRKVDWL TEKMHARDFT VSAMHGDMDQ
     KERDVIMREF RSGSSRVLIT TDLLARGIDV QQVSLVINYD LPTNRENYIH RIGRGGRFGR
     KGVAINMVTE EDKRTLRDIE TFYNTSIEEM PLNVADLI
//
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