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EIF3A_DROMO
ID   EIF3A_DROMO             Reviewed;        1129 AA.
AC   B4KA44;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=GI22072;
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22;
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; CH933806; EDW16719.1; -; Genomic_DNA.
DR   RefSeq; XP_002001258.2; XM_002001222.2.
DR   AlphaFoldDB; B4KA44; -.
DR   SMR; B4KA44; -.
DR   STRING; 7230.FBpp0171289; -.
DR   PRIDE; B4KA44; -.
DR   EnsemblMetazoa; FBtr0426343; FBpp0384039; FBgn0144801.
DR   GeneID; 6575244; -.
DR   KEGG; dmo:Dmoj_GI22072; -.
DR   eggNOG; KOG2072; Eukaryota.
DR   HOGENOM; CLU_002096_1_0_1; -.
DR   InParanoid; B4KA44; -.
DR   OMA; VMYQTTA; -.
DR   OrthoDB; 152929at2759; -.
DR   PhylomeDB; B4KA44; -.
DR   ChiTaRS; eIF3-S10; fly.
DR   Proteomes; UP000009192; 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   SMART; SM00088; PINT; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..1129
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   A"
FT                   /id="PRO_0000366338"
FT   DOMAIN          319..502
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          590..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..1129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..902
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        919..982
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        994..1079
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1099..1129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1129 AA;  133033 MW;  895692827C819EC3 CRC64;
     MARYTQRPEN ALKRANEFIE VGKPLRALDT LQEVFRNKRW NYAYSETVIE PLMFKYLYLC
     VELKKSHIAK EGLFQYRNMF QLVNVNSLEN VIRGYLKMAE EHTEAAQAQS SAAVAVLELD
     DLDNIATPES ILMSAVCGED AQDRSDRTIL LPWVKFLWES YCQCLELLRV NTHCEALYHD
     IARMAFQFCL KYNRKSEFRR LCDKLRKHLE DICKSSNQTT GVSINKVETQ QLCLDTRLYL
     LDSAIQMELW QEAYKAIEDI HGLMAMSKKT PVPKTMANYY QKLAMVFSKA GNQLFHAAAL
     LKLFQLTREL KKNLTKDDLQ RMAAHVLLAT LSIPLPSAHP EFDRFIEADK SPLEKAQKLA
     VLLGLPQPPT RVSLIREVVR LNVPNLVSED FRNLYNWLEV DFNPLNLCKR IQSIVDTIEA
     SETENTLLTP YIQSLKDVTI MRLIRQISQV YESIEFKRLL ELAPFCNIFE LEKLLVESVR
     HNDMQIRIDH QRNSIYFGTD LTESQREYRP DGPTLQSMPS EQIRSQLVNM STVLTRAVSI
     VYPNRERDQR AKLRSQMVQH YHEIKDREHQ RILQRQKIIE DRKEFIEKQN NAREEEEARR
     HEEESRKAKL AEQKRLEQEQ EERERKRHEN EIQAIKEKSL KEKVQQISQT AHGKKMLSKL
     DEEGIKKLDA EQIAMRESEE LQRERKELQS KLKSQEKKID YFERAKRLEE IPLFEKYLAE
     KNVKDKEFWE ATEATRIENA IAERKDAVSQ QERLKRMYPD RDEFLEALKK ERASLFVEKL
     KKFEIALAEE RKKRLAERVV RRREERRQAY LRAKEEERFR KEEEIRLARE AEERAAAEAR
     RLEREAEDEK RRQQYEKQRA KEEEAERKIQ EDRERLAREV AVERERSEKE RDVWRPRGDR
     SERPSAAPAG GASEWRRNAP TSDRNDRNDR NERNDRSDRN DRNDRSERIE RSDRNDRPER
     KDTDGGADSS WRVRREPVEP QRERGGGAGG GPSGRDDKWR RGGDRSERLG GDRDRDRDRD
     SFRRNDGPRR DDDRGGFRRD DQPQRDTGSN WRDSPRQNDR DNRDNRRPAG DRRDIRGAGP
     KEGGGGGGGG NWRTAPSPRD EKPPVKRDQP QDKENKAGDD GEWTSVKRR
 
 
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