ID   EIF3A_DROGR             Reviewed;         893 AA.
AC   B4K250;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000};
DE            Short=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 10 {ECO:0000255|HAMAP-Rule:MF_03000};
GN   Name=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
GN   Synonyms=eIF3-S10 {ECO:0000255|HAMAP-Rule:MF_03000}; ORFNames=GH11742;
OS   Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Hawaiian Drosophila.
OX   NCBI_TaxID=7222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15287-2541.00;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC       initiation factor 3 (eIF-3) complex, which is involved in protein
CC       synthesis of a specialized repertoire of mRNAs and, together with other
CC       initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC       the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation.
CC       {ECO:0000255|HAMAP-Rule:MF_03000}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. The eIF-3 complex interacts with pix.
CC       {ECO:0000255|HAMAP-Rule:MF_03000}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC       Rule:MF_03000}.
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DR   EMBL; CH918512; EDW04308.1; -; Genomic_DNA.
DR   RefSeq; XP_001997354.1; XM_001997318.1.
DR   AlphaFoldDB; B4K250; -.
DR   SMR; B4K250; -.
DR   STRING; 7222.FBpp0145648; -.
DR   EnsemblMetazoa; FBtr0465701; FBpp0415937; FBgn0119222.
DR   eggNOG; KOG2072; Eukaryota.
DR   HOGENOM; CLU_002096_2_1_1; -.
DR   InParanoid; B4K250; -.
DR   OMA; WGSRDDR; -.
DR   OrthoDB; 152929at2759; -.
DR   PhylomeDB; B4K250; -.
DR   ChiTaRS; eIF3-S10; fly.
DR   Proteomes; UP000001070; Unassembled WGS sequence.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR   HAMAP; MF_03000; eIF3a; 1.
DR   InterPro; IPR027512; EIF3A.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR14005; PTHR14005; 1.
DR   Pfam; PF01399; PCI; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..893
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   A"
FT                   /id="PRO_0000366336"
FT   DOMAIN          319..502
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          592..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          837..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          576..707
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COILED          784..881
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COMPBIAS        837..880
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   893 AA;  106035 MW;  81844FC247AE9FE0 CRC64;
     MARYTQRPEN ALKRANEFIE VGKPLRALDT LQEVFRNKRW NYTYSETVIE PLMFKYLYLC
     VELKKSHIAK EGLFQYRNMF QLVNVNSLEN VIRGYLKMAE EHTEAAQAQS SAAVAVLELD
     DLDNIATPES ILMSAVCGED AQDRSDRTIL LPWVKFLWES YCQCLELLRV NTHCEALYHD
     IARMAFQFCL KYNRKSEFRR LCDKLRKHLE DICKSNNQTT GVSITKPETQ QLCLDTRLYL
     LDSAIQMELW QEAYKAIEDI HGLMAMSKKT PVPKTMANYY QKLAMVFSKA GNQLFHAAAL
     LKLFQLTREL KKNLTKEDLQ RMAAHVLLAT LSIPLPSAHP EFDRFIEADK SPLEKAQKLA
     VLLGLPQPPT RVSLIRDVVR LNVPNLVSDE FRNLYNWLEV DFNPLNLCKR IQSIVDTIES
     TEKENTLLTP YIQSLKDVTI MRLIRQISQV YESIEFKRLL ELAPFCNIFE LEKLLVESVR
     HNDMQIRIDH QRNSIFFGTD LTESQREYRP DGPALQSMPS EQIRSQLVNM STVLTRAVSV
     VYPNRERDQR AKLRTQMVQH YHEIKDREHQ RILQRQKIIE DRKEFIEKQN NARELEEARR
     HEDESRKAKQ AEQKRLEQEQ EKRERKRHEN EIQAIKEKSL KEKVQQISQT AHGKKMLSKL
     DEEGIKKLDA EQIAMRESEE LQRERKELQS KIKSQEKKID YFERAKRLEE IPLFEKYLAE
     KNVKDKEFWE STEQTRIELD IAERKDAVAQ QARLQRMYPD RDEYLNALKK ERASLYVEKL
     KKFEIALAEE RKKRLADRIV RRREERRQAY LRAKEEERFR KEEEIRHARE AEERAAAEAR
     RLEREAEDEK RRQQYEKQRA KEEEAERKIQ EDRDRLAREV AVEPSTCFSR RRQ