ID   EIF3K_DROAN             Reviewed;         222 AA.
AC   B3MIY7;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit K {ECO:0000255|HAMAP-Rule:MF_03010};
DE            Short=eIF3k {ECO:0000255|HAMAP-Rule:MF_03010};
DE   AltName: Full=eIF-3 p25 {ECO:0000255|HAMAP-Rule:MF_03010};
GN   ORFNames=GF13261;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13;
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: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is involved in protein synthesis of a
CC       specialized repertoire of mRNAs and, together with other initiation
CC       factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC       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_03010}.
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_03010}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03010}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit K family. {ECO:0000255|HAMAP-
CC       Rule:MF_03010}.
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DR   EMBL; CH902619; EDV37053.1; -; Genomic_DNA.
DR   RefSeq; XP_001960231.1; XM_001960195.2.
DR   AlphaFoldDB; B3MIY7; -.
DR   SMR; B3MIY7; -.
DR   STRING; 7217.FBpp0116453; -.
DR   EnsemblMetazoa; FBtr0117961; FBpp0116453; FBgn0090293.
DR   GeneID; 6496103; -.
DR   KEGG; dan:6496103; -.
DR   eggNOG; KOG3252; Eukaryota.
DR   HOGENOM; CLU_076723_1_0_1; -.
DR   InParanoid; B3MIY7; -.
DR   OMA; WKHQGQG; -.
DR   OrthoDB; 1576799at2759; -.
DR   PhylomeDB; B3MIY7; -.
DR   Proteomes; UP000007801; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; 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; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.25.40.250; -; 1.
DR   HAMAP; MF_03010; eIF3k; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR033464; CSN8_PSD8_EIF3K.
DR   InterPro; IPR009374; eIF3k.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR016020; Transl_init_fac_sub12_N_euk.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13022; PTHR13022; 1.
DR   Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..222
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   K"
FT                   /id="PRO_0000365040"
FT   DOMAIN          46..208
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ   SEQUENCE   222 AA;  25686 MW;  79538C34D30CFEA7 CRC64;
     MSHLVKMENG QSQTIQEMLG CIERYNPDHL KTLEAYVQDQ AKNNTYDLEA NLAVLKLYQF
     NPHMLNFDIT YTILLKCLTN LPHTDFVMAK CLLLPQQMKD ENVQTIIDLA DILERADFTL
     FWQRAEVNRN MFRHITGFHD SIRKFVSHVI GTTFQTIRKD LLKELLGGIE DSTLESWVKR
     NGWKHQGQGL VVVATQDDKI KTKNITEKIE FENVGALMAQ CL