ID   EI3D1_DROSI             Reviewed;         560 AA.
AC   B4R222;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit D-1 {ECO:0000255|HAMAP-Rule:MF_03003};
DE            Short=eIF3d-1 {ECO:0000255|HAMAP-Rule:MF_03003};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 7-1 {ECO:0000255|HAMAP-Rule:MF_03003};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit p66;
GN   Name=eIF3d1 {ECO:0000255|HAMAP-Rule:MF_03003}; Synonyms=eIF-3p66;
GN   ORFNames=GD21022;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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: mRNA cap-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. In the
CC       eIF-3 complex, eif3d specifically recognizes and binds the 7-
CC       methylguanosine cap of a subset of mRNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_03003}.
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_03003}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}.
CC   -!- DOMAIN: The RNA gate region regulates mRNA cap recognition to prevent
CC       promiscuous mRNA-binding before assembly of eif3d into the full
CC       eukaryotic translation initiation factor 3 (eIF-3) complex.
CC       {ECO:0000255|HAMAP-Rule:MF_03003}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit D family. {ECO:0000255|HAMAP-
CC       Rule:MF_03003}.
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DR   EMBL; CM000364; EDX14079.1; -; Genomic_DNA.
DR   RefSeq; XP_002104576.1; XM_002104540.2.
DR   AlphaFoldDB; B4R222; -.
DR   SMR; B4R222; -.
DR   STRING; 7240.B4R222; -.
DR   EnsemblMetazoa; FBtr0220932; FBpp0219424; FBgn0192477.
DR   GeneID; 6729256; -.
DR   HOGENOM; CLU_024521_2_0_1; -.
DR   OMA; PDGWGPC; -.
DR   PhylomeDB; B4R222; -.
DR   ChiTaRS; eIF-3p66; fly.
DR   Proteomes; UP000000304; Chromosome 3r.
DR   Bgee; FBgn0192477; Expressed in embryo and 3 other tissues.
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:0005634; C:nucleus; IEA:EnsemblMetazoa.
DR   GO; GO:0098808; F:mRNA cap binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR   GO; GO:0002191; P:cap-dependent translational initiation; IEA:UniProtKB-UniRule.
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_03003; eIF3d; 1.
DR   InterPro; IPR007783; eIF3d.
DR   PANTHER; PTHR12399; PTHR12399; 1.
DR   Pfam; PF05091; eIF-3_zeta; 1.
DR   PIRSF; PIRSF016281; EIF-3_zeta; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..560
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   D-1"
FT                   /id="PRO_0000364158"
FT   REGION          98..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..305
FT                   /note="RNA gate"
FT                   /evidence="ECO:0000250|UniProtKB:K7IM66"
FT   COMPBIAS        102..116
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         128
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   560 AA;  63772 MW;  C3A650A262D1B7F0 CRC64;
     MSETINTAAQ FPSFEKPTVQ FNEKGWGPCE LPDTFKDVPY QPFSKNDRLG KICDWTNTSS
     NDKKYQNKYA SSFGTGNQYS YYHEEDETTF HLVDTARVQK PPHQRGRFRN MRNSRSGRGR
     NARGGLNTHG MTTLSGKNVK ARDPRHGRGM GKKFGHRGPP PKMRESSVAV RADWASIEEM
     DFPRLIKLSL PNIKEGVDIV TCGTLEYYDK TYDRINVKNE KPLQKIDRIV HTVTTTDDPV
     IRRLSKTVGN VFATDAILAT IMCSTRSNYS WDIVIEKVGD KVFMDKRDHT EFDLLTVNES
     SVEPPTDDDS SCNSPRNLAI EATFINHNFS QQVLKTGDQE PKYKFEESNP FISEDEDIQV
     ASVGYRYKKW ELGSDIVLVA RCEHDGVLQT PSGEPQFMTI KALNEWDSKL ANGVEWRQKL
     DTQRGAVLAN ELRNNACKLA KWTVQAVLAG SDQLKLGYVS RINPRDHSRH VILGTQQFKP
     HEFATQINLS MDNAWGILRC IIDLVMKQKD GKYLIMKDPN KPIIRLYDIP DNTFDSDDSD
     DGEGDDEGFQ QVYNYAHNKI