EI3D1_DROYA
ID EI3D1_DROYA Reviewed; 560 AA.
AC B4PNV2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=GE10378;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
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; CM000160; EDW98162.1; -; Genomic_DNA.
DR RefSeq; XP_002098450.1; XM_002098414.2.
DR AlphaFoldDB; B4PNV2; -.
DR SMR; B4PNV2; -.
DR STRING; 7245.FBpp0255388; -.
DR EnsemblMetazoa; FBtr0256896; FBpp0255388; FBgn0228244.
DR GeneID; 6537910; -.
DR KEGG; dya:Dyak_GE10378; -.
DR eggNOG; KOG2479; Eukaryota.
DR HOGENOM; CLU_024521_2_0_1; -.
DR OMA; PDGWGPC; -.
DR OrthoDB; 1030308at2759; -.
DR PhylomeDB; B4PNV2; -.
DR ChiTaRS; eIF-3p66; fly.
DR Proteomes; UP000002282; Chromosome 3R.
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 RNA-binding.
FT CHAIN 1..560
FT /note="Eukaryotic translation initiation factor 3 subunit
FT D-1"
FT /id="PRO_0000364164"
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; 63788 MW; E94257FD42BFBF0D CRC64;
MSETINTAAQ FPSFEKPTVQ FNEKGWGPCE LPDTFKDVPY QPFSKNDRLG KICDWTNTSN
NDKKYQNKYA SSFGTGNQYS YYHEEDETTF HLVDTARVQK PPHQRGRFRN MRNSRSGRGR
NARGGLNTHG MTTLSGKNVK ARDPRHGRGM GKKFGHRGPP PKMRESSVAV RADWASIEEM
DFPRLIKLSL PNIKEGVDIV TCGTLEYYDK TYDRINVKNE KPLQKIDRIV HTVTTTDDPV
IRRLSKTVGN VFATDAILAT IMCSTRSNYS WDIVIEKVGD KIFMDKRDHT EFDLLTVNES
SVEPPTDDDS SCNSPRNLAI EATFINHNFS QQVLKTGDQE PKYKFEESNP FISEDEDIQV
ASVGYRYKKW ELGSDIVLVA RCEHDGVLQT PSGDSQFMTI KALNEWDSKL ANGVEWRQKL
DTQRGAVLAN ELRNNACKLA KWTVQAVLAG SDQLKLGYVS RINPRDHSRH VILGTQQFKP
HEFATQINLS MDNAWGILRC IIDLVMKQKD GKYLIMKDPN KPIIRLYDIP DNTFDSDDSD
DGEGDDEGFQ QVYNYAHNKI
